|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
16-324 |
1.26e-137 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 392.43 E-value: 1.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKG---CKHFVCSTGGNAGFATAYAAKKLRIPATIIV 92
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 93 PTSTPQATVQKLEEQGTEVQVFGKVWDDAyAKALA--LADTE-GWVSVHPFDHPLIWQGHASMVRELKDLLG--HKPGAI 167
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWWEA-DNYLReeLAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQsqEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 168 VLAVGGGGLLAGVVAGLQDVGWQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAKTVSARALECASECQVIS 247
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820684309 248 QLVEDVEAVQAVELFLDDERMLVQPACGAPLALLYMGRVQQLQREGHLNPDlDSIVVIVCGGSSIQLAGLQALKTQL 324
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLTPL-DNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
10-309 |
2.37e-59 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 193.33 E-value: 2.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 10 REFHILTPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGiGYFC-----QEAAKKGckhFVCSTGGNAGFATAYAAKKL 84
Cdd:COG1171 19 AGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRG-AYNAlaslsEEERARG---VVAASAGNHAQGVAYAARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 85 RIPATIIVPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHkp 164
Cdd:COG1171 95 GIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLPD-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 165 gaivlavggggllagvvaglQD-----VG---------------WQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVA 224
Cdd:COG1171 173 --------------------LDavfvpVGgggliagvaaalkalSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 225 KCLGAKTVSARALECASEC--QVIsqLVEDVEAVQAVELFLDDERMLVQPACGAPLALLYMGRVqQLQREghlnpdldSI 302
Cdd:COG1171 233 DGLAVGRPGELTFEILRDLvdDIV--TVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKE-RLKGK--------RV 301
|
....*..
gi 1820684309 303 VVIVCGG 309
Cdd:COG1171 302 VVVLSGG 308
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
16-308 |
7.70e-56 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 183.28 E-value: 7.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIgYFCQEAAKKGCK--HFVCSTGGNAGFATAYAAKKLRIPATIIVP 93
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGA-LNLLLRLKEGEGgkTVVEASSGNHGRALAAAAARLGLKVTIVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 94 TSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALA-DTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKPGAIVLAVG 172
Cdd:pfam00291 87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 173 GGGLLAGVVAGLQDvGWQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAK-TVSARALECASECQVISQLVE 251
Cdd:pfam00291 167 GGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVGEVVTVS 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820684309 252 DVEAVQAVELFLDDERMLVQPACGAPLALLymgrvqQLQREGHLNPDlDSIVVIVCG 308
Cdd:pfam00291 246 DEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELKGG-DRVVVVLTG 295
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
16-309 |
1.40e-52 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 174.98 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGckhFVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPATIV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHAS----MVRELKDL------LG 161
Cdd:cd01562 95 MPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTigleILEQVPDLdavfvpVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 162 --------------HKPgaivlavggggllagvvaglqdvgwqDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCL 227
Cdd:cd01562 175 gggliagiatavkaLSP--------------------------NTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 228 GAKTVSARALEcasecqVISQLVEDV------EAVQAVELFLDDERMLVQPACGAPLALLYMGRVQQLQReghlnpdldS 301
Cdd:cd01562 229 AVKRPGELTFE------IIRKLVDDVvtvsedEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGK---------K 293
|
....*...
gi 1820684309 302 IVVIVCGG 309
Cdd:cd01562 294 VVVVLSGG 301
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
16-309 |
2.66e-49 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 164.61 E-value: 2.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKG---CKHFVCSTGGNAGFATAYAAKKLRIPATIIV 92
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 93 PTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALA-DTEGWVSVHPFDHPLIWQGHASMVRELKdllghkpgaivlav 171
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAeEDPGAYYVNQFDNPANIAGQGTIGLEIL-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 172 ggggllagvvaglQDVGWQDVPIIAVETKGADSFNA---ALKAGrlvtLPEITSVAkclgaktVSARALecasecqvisq 248
Cdd:cd00640 147 -------------EQLGGQKPDAVVVPVGGGGNIAGiarALKEL----LPNVKVIG-------VEPEVV----------- 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820684309 249 LVEDVEAVQAVELFLDDERMLVQPACGAPLALLYmgrvqQLQREGhlnPDLDSIVVIVCGG 309
Cdd:cd00640 192 TVSDEEALEAIRLLAREEGILVEPSSAAALAAAL-----KLAKKL---GKGKTVVVILTGG 244
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
16-309 |
7.93e-40 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 142.02 E-value: 7.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTkVYMKLENVQPTGSFKIRGIGYFcQEAAKKGCKHFVCSTGGNAGFATAYAAKKLRIPATIIVPTS 95
Cdd:PRK08246 24 TPVLEADGAGFGPAP-VWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 96 TPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKP---------GA 166
Cdd:PRK08246 102 APPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDtvlvavgggGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 167 IVLAVggggllagvvaglqdvGW--QDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAKTVSARALECASECQ 244
Cdd:PRK08246 182 IAGIA----------------AWfeGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHV 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820684309 245 VISQLVEDVEAVQAVELFLDDERMLVQPACGAPLALLYMGRVQQLQREghlnpdldSIVVIVCGG 309
Cdd:PRK08246 246 VTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
16-309 |
5.30e-38 |
|
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130197 [Multi-domain] Cd Length: 380 Bit Score: 139.11 E-value: 5.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGCkhfVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANLSEDQRQRGV---VAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKPGAIVLAV 171
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 172 GGGGLLAGVVAGLQDVgwQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAKTVSARALECASEC--QVISql 249
Cdd:TIGR01127 158 GGGLISGVASAAKQIN--PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYvdDVVT-- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 250 VEDVEAVQAVELFLDDERMLVQPACGAPLALLYmgrvqqlqrEGHLNPDLDSIVVIVCGG 309
Cdd:TIGR01127 234 VDEEEIANAIYLLLERHKILAEGAGAAGVAALL---------EQKVDVKGKKIAVVLSGG 284
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
14-308 |
6.80e-32 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 124.46 E-value: 6.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 14 ILTPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGckhFVCSTGGNAGFATAYAAKKLRIPAT 89
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGaynkMAQLSPEQKARG---VIAASAGNHAQGVAFSAARLGLKAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 90 IIVPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKPGAIVL 169
Cdd:TIGR01124 93 IVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 170 AVGGGGLLAGVVAGLQDVGWQdVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAKTVSARALECaseCQvisQL 249
Cdd:TIGR01124 173 PVGGGGLAAGVAALIKQLMPE-IKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRL---CQ---QY 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820684309 250 VEDV------EAVQAVELFLDDERMLVQPAcGApLALlyMGRVQQLQREGHLNPDLdsiVVIVCG 308
Cdd:TIGR01124 246 LDDIvtvdtdEVCAAIKDLFEDTRAVAEPA-GA-LAL--AGLKKYVALHGIRGQTL---VAILSG 303
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
16-308 |
2.69e-31 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 122.55 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPvLESAA-LSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGCkhfVCSTGGNAGFATAYAAKKLRIPATI 90
Cdd:PRK09224 21 TP-LEKAPkLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAVI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 91 IVPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKPGAIVLA 170
Cdd:PRK09224 97 VMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVFVP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 171 VGGGGLLAGVVAGLQDVgWQDVPIIAVETKGADSFNAALKAGRLVTLPEI------TSVaKCLGAKTVsaralecasecQ 244
Cdd:PRK09224 177 VGGGGLIAGVAAYIKQL-RPEIKVIGVEPEDSACLKAALEAGERVDLPQVglfadgVAV-KRIGEETF-----------R 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820684309 245 VISQLVEDVEAVQ------AVELFLDDERMLVQPAcGApLALLYMGR-VQQLQREGHlnpdldSIVVIVCG 308
Cdd:PRK09224 244 LCQEYVDDVITVDtdeicaAIKDVFEDTRSIAEPA-GA-LALAGLKKyVAQHGIEGE------TLVAILSG 306
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
16-231 |
1.46e-30 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 119.53 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYF-CQEAAKKGCKHFVCSTGGNAGFATAYAAKKLRIPATIIVPT 94
Cdd:PRK08639 26 TPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGVIFMPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 95 STPQATVQKLEEQG---TEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLG--HKPGAIVL 169
Cdd:PRK08639 106 TTPQQKIDQVRFFGgefVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEkeGSPDYVFV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820684309 170 AVGGGGLLAGVVAGLQDVGWQdVPIIAVETKGADSFNAALKAGRLVTLPEI------TSVAKcLGAKT 231
Cdd:PRK08639 186 PVGGGGLISGVTTYLKERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIdkfvdgAAVAR-VGDLT 251
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
16-293 |
4.45e-30 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 119.52 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGCkhfVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGaynkMARLPAEQLARGV---ITASAGNHAQGVALAAARLGVKAVIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRElkdLLGHKPGAIVLAV 171
Cdd:PRK12483 115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAME---ILRQHPGPLDAIF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 172 GGGGLLAGVVAGLQDVGW--QDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAKTVSARALEcasecqVISQL 249
Cdd:PRK12483 192 VPVGGGGLIAGIAAYVKYvrPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFE------LCRHY 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1820684309 250 VEDVEAVQAVEL------FLDDERMLVQPACgaplALLYMGRVQQLQREG 293
Cdd:PRK12483 266 VDEVVTVSTDELcaaikdIYDDTRSITEPAG----ALAVAGIKKYAEREG 311
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
16-160 |
1.21e-28 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 112.37 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFV--CSTGgNAGFATAYAAKKLRIPATIIVP 93
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVvtASTG-NHGRALAYAARALGIRATICMS 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820684309 94 TSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLL 160
Cdd:PRK07476 99 RLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEAL 165
|
|
| PLN02970 |
PLN02970 |
serine racemase |
16-317 |
2.02e-24 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 101.29 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGCkhfVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVqvfgkVWDDAY-----AKALALADTEGWVSVHPFDHPLIWQGHAS----MVRELKDLlgh 162
Cdd:PLN02970 105 VPKNAPACKVDAVIRYGGII-----TWCEPTvesreAVAARVQQETGAVLIHPYNDGRVISGQGTialeFLEQVPEL--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 163 kpGAIVLAVGGGGLLAGVVAGLQDVGwQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKclGAKTvSARALECAse 242
Cdd:PLN02970 177 --DVIIVPISGGGLISGIALAAKAIK-PSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIAD--GLRA-SLGDLTWP-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 243 cqVISQLVEDV------EAVQAVELFLDDERMLVQPACGAPLALLYMGRVQQ-LQREGHLNpdldsIVVIVCGGsSIQLA 315
Cdd:PLN02970 249 --VVRDLVDDVitvddkEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSnPAWKGCKN-----VGIVLSGG-NVDLG 320
|
..
gi 1820684309 316 GL 317
Cdd:PLN02970 321 VL 322
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
16-281 |
3.06e-24 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 101.89 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGCkhfVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:PRK07334 24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGalnkLLLLTEEERARGV---IAMSAGNHAQGVAYHAQRLGIPATIV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRE-LKD------------ 158
Cdd:PRK07334 101 MPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEmLEDapdldtlvvpig 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 159 ---LLG--------HKPgaivlavggggllagvvaglqdvgwqDVPIIAVETKGADSFNAALKAgrlVTLPEITS-VAKC 226
Cdd:PRK07334 181 gggLISgmataakaLKP--------------------------DIEIIGVQTELYPSMYAAIKG---VALPCGGStIAEG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820684309 227 LGAKTVSARALEcasecqVISQLVEDVEAV------QAVELFLDDERMLVQPACGAPLALL 281
Cdd:PRK07334 232 IAVKQPGQLTLE------IVRRLVDDILLVseadieQAVSLLLEIEKTVVEGAGAAGLAAL 286
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
15-167 |
1.55e-23 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 98.69 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 15 LTPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGC--KHFVCSTGGNAGFATAYAAKKLRIPATIIV 92
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYSTGNHGQAVAYASKLFGIKTRIYL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820684309 93 PTSTPQATVQKLEEQGTEVQVFgKVWDDAYAKAlALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKPGAI 167
Cdd:PRK06608 103 PLNTSKVKQQAALYYGGEVILT-NTRQEAEEKA-KEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAI 175
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
16-319 |
3.03e-23 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 97.84 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGckhFVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGhKPGAIVLAV 171
Cdd:PRK06815 98 APEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQP-DLDAVFVAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 172 GGGGLLAGVVAGLQDVGwQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLgAKTVSARALECASECQVISQ--L 249
Cdd:PRK06815 177 GGGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGT-AGGVEPGAITFPLCQQLIDQkvL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 250 VEDVEAVQAVELFLDDERMLVQPACGAPLALLymgrvQQLQREGHLNPdldsIVVIVCgGSSIQLAGLQA 319
Cdd:PRK06815 255 VSEEEIKEAMRLIAETDRWLIEGAAGVALAAA-----LKLAPRYQGKK----VAVVLC-GKNIVLEKYLE 314
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
16-159 |
2.83e-22 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 95.19 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGckhFVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKVV 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRE-LKDL 159
Cdd:PRK08638 105 MPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEiLEDL 173
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
14-279 |
1.92e-20 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 91.91 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 14 ILTPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGCkhfVCSTGGNAGFATAYAAKKLRIPAT 89
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGaynmMAKLPKEQLDKGV---ICSSAGNHAQGVALSAQRLGCDAV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 90 IIVPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKPGAIVL 169
Cdd:PLN02550 185 IAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 170 AVGGGGLLAGVVAGLQDVGwQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAKTVSARALECASECQVISQL 249
Cdd:PLN02550 265 PVGGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVL 343
|
250 260 270
....*....|....*....|....*....|
gi 1820684309 250 VEDVEAVQAVELFLDDERMLVQPACGAPLA 279
Cdd:PLN02550 344 VSRDAICASIKDMFEEKRSILEPAGALALA 373
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
16-161 |
2.22e-19 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 87.00 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG----IGYFCQEAAKKGCKHFvcsTGGNAGFATAYAAKKLRIPATII 91
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAGVVTF---SSGNHAQAIALSARLLGIPATIV 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 92 VPTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLG 161
Cdd:PRK07048 102 MPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVG 171
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
16-228 |
3.15e-19 |
|
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.
Pssm-ID: 132036 [Multi-domain] Cd Length: 317 Bit Score: 86.45 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG-IGYFCQEAAKKGCKHFVCSTGGNAGFATAYAAKKLRIPATIIVPT 94
Cdd:TIGR02991 20 TPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGaTNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMSE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 95 STPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHAS----MVRELKDLlghkpgAIVLA 170
Cdd:TIGR02991 100 LVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTlgleVVEQMPDL------ATVLV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1820684309 171 VGGGGLLAGVVAGLQDVGWQDVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCLG 228
Cdd:TIGR02991 174 PLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLG 231
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
32-261 |
1.45e-17 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 82.37 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 32 VYMKLENVQPTGSFKIRGIGYFCQEAAKKG-CKHFVCSTGGNAGFATAYAAKKLRIPATIIVPTSTPQATVQKLEEQGTE 110
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGdERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 111 VQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKdllGHKPGAIVLAVGGGGLLAGVVAGLQDvgwQ 190
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELA---AHAPDVVIVPIGGGGLASGVALALKS---Q 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820684309 191 DVPIIAVETKGADSFNAALKAgrlvTLPEITSVAKCLGAKTVSARALECASECqviSQLVEDVEAVQAVEL 261
Cdd:PRK08813 204 GVRVVGAQVEGVDSMARAIRG----DLREIAPVATLADGVKVKIPGFLTRRLC---SSLLDDVVIVREAEL 267
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
16-308 |
1.62e-17 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 82.56 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFATA-YAAKKlRIPATIIVP- 93
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAaYAARA-GIEVFVFVPe 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 94 TSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFdHPL-----------IWQ-------------GH 149
Cdd:COG0498 146 GKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPArlegqktyafeIAEqlgrvpdwvvvptGN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 150 ASMV-------RELKDLlghkpgaivlavggggllagvvaglqdvGWQD-VP-IIAVETKGADSFNAALKAGRLVTLPEi 220
Cdd:COG0498 225 GGNIlagykafKELKEL----------------------------GLIDrLPrLIAVQATGCNPILTAFETGRDEYEPE- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 221 tsvakclGAKTVS-----------ARALECASECQVISQLVEDVEAVQAVELFLDDERMLVQPACGAPLALLymgrvQQL 289
Cdd:COG0498 276 -------RPETIApsmdignpsngERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGL-----RKL 343
|
330
....*....|....*....
gi 1820684309 290 QREGHLNPDlDSIVVIVCG 308
Cdd:COG0498 344 REEGEIDPD-EPVVVLSTG 361
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
15-167 |
3.72e-17 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 81.20 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 15 LTPVLESAALSKAAG-TKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFA-TAYAAKKlRIPATIIV 92
Cdd:PRK08197 79 MTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAwAAYAARA-GIRATIFM 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820684309 93 PTSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHK-PGAI 167
Cdd:PRK08197 158 PADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGWRlPDVI 233
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
16-308 |
1.92e-15 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 75.71 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTK-VYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFATA-YAAKKlRIPATIIVP 93
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTGNTSASLAaYAARA-GIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 94 TSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADtEGWVSVHPFDHPLIWQGHASMVRELKDLLGHK-------P-- 164
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAE-ENWIYLSNSLNPYRLEGQKTIAFEIAEQLGWEvpdyvvvPvg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 165 --GAIvlavgggGLLAGVVAGLQDVGWQD-VP-IIAVETKGADSFNAALKAGRLVTLPEITSVAKCLGAKT---VSA-RA 236
Cdd:cd01563 181 ngGNI-------TAIWKGFKELKELGLIDrLPrMVGVQAEGAAPIVRAFKEGKDDIEPVENPETIATAIRIgnpASGpKA 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820684309 237 LECASECQVISQLVEDVEAVQAVELFLDDERMLVQPACGAPLALLymgrvQQLQREGHLNPDlDSIVVIVCG 308
Cdd:cd01563 254 LRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGL-----KKLREEGIIDKG-ERVVVVLTG 319
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
16-279 |
6.05e-15 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 74.26 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRG-IGYFCQEAAKK-GCKHFVCSTGGNAGFATAYAAKKLRIPATIIVP 93
Cdd:PRK06110 22 TPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGgLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 94 TSTPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFdHPLIWQGHASMVREL----------------- 156
Cdd:PRK06110 102 HGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELfravpdldvvyvpigmg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 157 ---------KDLLGHKpgaivlavggggllagvvaglqdvgwqdVPIIAVETKGADSFNAALKAGRLVTLPEITSVAKCL 227
Cdd:PRK06110 181 sgicgaiaaRDALGLK----------------------------TRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGM 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1820684309 228 GAKTVSARALECASE--CQVISqlVEDVEAVQAVELFLDDERMLVQPACGAPLA 279
Cdd:PRK06110 233 ACRTPDPEALEVIRAgaDRIVR--VTDDEVAAAMRAYFTDTHNVAEGAGAAALA 284
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
16-149 |
2.78e-11 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 63.30 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGC----KHFVCSTGGNAGFATAYAAKKLRIPATII 91
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820684309 92 VPTSTPQATVQKLEEQGTEV-QVFGKVWDD---AYAKALALA-DTEGWVSVHPFDHPLIWQGH 149
Cdd:cd01561 83 MPETMSEEKRKLLRALGAEViLTPEAEADGmkgAIAKARELAaETPNAFWLNQFENPANPEAH 145
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
16-167 |
3.56e-11 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 63.19 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAG-TKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFATAYAAKKLRIPATIIVPT 94
Cdd:PRK06381 16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820684309 95 STPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFD-HPLI-WQGHASMVRELKDLLGHKPGAI 167
Cdd:PRK06381 96 SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSvNSVVdIEAYSAIAYEIYEALGDVPDAV 170
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
16-149 |
8.00e-10 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 58.91 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRgIGYFCQEAA------KKGcKHFVCSTGGNAGFATAYAAKKLRIPAT 89
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDR-IALSMIEDAekrgllKPG-GTIVEATSGNTGIGLAMVAAAKGYRLI 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820684309 90 IIVPTSTPQATVQKLEEQGTEVQVFGKV--WDDAYAKALALAD-TEGWVSVHPFDHPLIWQGH 149
Cdd:COG0031 92 LVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAAeTPGAFWPNQFENPANPEAH 154
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
16-156 |
2.74e-09 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 57.90 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLEsAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFATAYAAKKLRIPATIIVPTS 95
Cdd:PRK05638 67 TPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820684309 96 TPQATVQKLEEQGTEVQVFGKVWDDAYAKALALADTEGWVSVHPFDHPLIWQGHASMVREL 156
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFEL 206
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
15-111 |
7.84e-07 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 50.21 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 15 LTPVLEsaalskaAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFATAYAAKKLRIPATIIVPT 94
Cdd:PRK08329 64 ITPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSY 136
|
90
....*....|....*..
gi 1820684309 95 STPQATVQKLEEQGTEV 111
Cdd:PRK08329 137 NASKEKISLLSRLGAEL 153
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
16-305 |
1.28e-05 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 46.22 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGTK-VYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFATA-YAAKKlRIPATIIVP 93
Cdd:TIGR00260 23 TPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAaYAGKA-GLKVVVLYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 94 TSTPQA--TVQKLEEQGTEVQVFGKvWDDAYAKALALADTE---GWVSVHpfdhpLIW---QGHASMVRELKDLLGHK-P 164
Cdd:TIGR00260 102 AGKISLgkLAQALGYNAEVVAIDGN-FDDAQRLVKQLFEDKpalGLNSAN-----SIPyrlEGQKTYAFEAVEQLGWEaP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 165 GAIVLAVGGG---GLLAGVVAGLQDVGWQDVPI-IAVETKGA-DSFNAALKAGRLVTL--PEITSVAKCLGAKTVSARAL 237
Cdd:TIGR00260 176 DKVVVPVPNSgnfGAIWKGFKEKKMLGLDSLPVkRGIQAEGAaDIVRAFLEGGQWEPIetPETLSTAMDIGNPANWPRAL 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820684309 238 ECASECQVISQLVEDVEAVQAVELFLDDERMLVQPACGAPLALLymgrvQQLQREGHLNPDLDSIVVI 305
Cdd:TIGR00260 256 EAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAAL-----LKLVEKGTADPAERVVCAL 318
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
29-164 |
1.60e-05 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 45.88 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 29 GTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTGGNAGFATAYAAKKLRIPATIIVPTSTPQATVQKLEEQG 108
Cdd:PRK06450 64 KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYG 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1820684309 109 TEV-QVFGKVWDDAYAkalalADTEGWVSVHPFDHPLIWQGHASMVRELKDLLGHKP 164
Cdd:PRK06450 144 AEVvRVRGSREDVAKA-----AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKI 195
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
16-90 |
2.71e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 42.49 E-value: 2.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820684309 16 TPVLESAALSKAAGTKVYMKLENVQPTGSFKIRGIGYFCQEAAKKGCKHFVCSTG-GNAGFATAYAAKKLRIPATI 90
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTRIIAETGaGQHGVATATACALFGLKCTI 347
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
16-90 |
4.62e-04 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 41.37 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAA-GTKVYMKLENVQPTGSFKIR---GIGYFcqeAAKKGCKHFVCSTG-GNAGFATAYAAKKLRIPATI 90
Cdd:cd06446 35 TPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKINnalGQALL---AKRMGKKRVIAETGaGQHGVATATACALFGLECEI 111
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
16-84 |
1.60e-03 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 39.71 E-value: 1.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820684309 16 TPVLESAALSKAAGTKV--YMKLENVQPTGSF---KIRGIGYFCQEAAKKGCKHFVcSTGG---NAGFATAYAAKKL 84
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVeiYAKRDDCNSGLAFggnKIRKLEYLLPDALAKGADTLV-TVGGiqsNHTRQVAAVAAKL 76
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
16-90 |
1.82e-03 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 39.78 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820684309 16 TPVLESAALSKAAGT--KVYMKLENVQPTGSFKIRGI---GYFcqeAAKKGCKHFVCSTG-GNAGFATAYAAKKLRIPAT 89
Cdd:PRK12391 78 TPLIRARRLEKALGTpaKIYYKYEGVSPTGSHKPNTAvaqAYY---NKKEGIKRLTTETGaGQWGSALALACALFGLECT 154
|
.
gi 1820684309 90 I 90
Cdd:PRK12391 155 V 155
|
|
| |
