ID NANE_STAA8 Reviewed; 222 AA.
AC Q2G157;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
DE EC=5.1.3.9 {ECO:0000255|HAMAP-Rule:MF_01235};
DE AltName: Full=ManNAc-6-P epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
GN Name=nanE {ECO:0000255|HAMAP-Rule:MF_01235};
GN OrderedLocusNames=SAOUHSC_00298;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
CC -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000255|HAMAP-
CC Rule:MF_01235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine
CC 6-phosphate; Xref=Rhea:RHEA:23932, ChEBI:CHEBI:57599,
CC ChEBI:CHEBI:57666; EC=5.1.3.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01235};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC {ECO:0000255|HAMAP-Rule:MF_01235}.
CC -!- SIMILARITY: Belongs to the NanE family. {ECO:0000255|HAMAP-
CC Rule:MF_01235}.
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DR EMBL; CP000253; ABD29467.1; -; Genomic_DNA.
DR RefSeq; WP_000936720.1; NZ_LS483365.1.
DR RefSeq; YP_498888.1; NC_007795.1.
DR PDB; 6VVA; X-ray; 1.84 A; A/B=1-222.
DR PDBsum; 6VVA; -.
DR AlphaFoldDB; Q2G157; -.
DR SMR; Q2G157; -.
DR STRING; 93061.SAOUHSC_00298; -.
DR PaxDb; 1280-SAXN108_0302; -.
DR GeneID; 3919525; -.
DR KEGG; sao:SAOUHSC_00298; -.
DR PATRIC; fig|93061.5.peg.271; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_1_0_9; -.
DR OrthoDB; 9781704at2; -.
DR UniPathway; UPA00629; UER00682.
DR PRO; PR:Q2G157; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0009385; F:N-acylmannosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006053; P:N-acetylmannosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR CDD; cd04729; NanE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01235; ManNAc6P_epimer; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007260; NanE.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR36204; N-ACETYLMANNOSAMINE-6-PHOSPHATE 2-EPIMERASE-RELATED; 1.
DR PANTHER; PTHR36204:SF1; N-ACETYLMANNOSAMINE-6-PHOSPHATE 2-EPIMERASE-RELATED; 1.
DR Pfam; PF04131; NanE; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..222
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000301485"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6VVA"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:6VVA"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6VVA"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:6VVA"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6VVA"
SQ SEQUENCE 222 AA; 24545 MW; 7417D8DD1A48A041 CRC64;
MLPHGLIVSC QALPDEPLHS SFIMSKMALA AYEGGAVGIR ANTKEDILAI KETVDLPVIG
IVKRDYDHSD VFITATSKEV DELIESQCEV IALDATLQQR PKETLDELVS YIRTHAPNVE
IMADIATVEE AKNAARLGFD YIGTTLHGYT SYTQGQLLYQ NDFQFLKDVL QSVDAKVIAE
GNVITPDMYK RVMDLGVHCS VVGGAITRPK EITKRFVQIM ED
//
