ID NANE_FUSNN Reviewed; 224 AA.
AC Q8RDN5;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 110.
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}; OrderedLocusNames=FN1476;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL95669.1; -; Genomic_DNA.
DR RefSeq; NP_604370.1; NC_003454.1.
DR RefSeq; WP_011017182.1; NZ_CP028101.1.
DR PDB; 5ZKN; X-ray; 2.21 A; A=1-224.
DR PDBsum; 5ZKN; -.
DR AlphaFoldDB; Q8RDN5; -.
DR SMR; Q8RDN5; -.
DR STRING; 190304.FN1476; -.
DR PaxDb; 190304-FN1476; -.
DR EnsemblBacteria; AAL95669; AAL95669; FN1476.
DR GeneID; 79784439; -.
DR KEGG; fnu:FN1476; -.
DR PATRIC; fig|190304.8.peg.2036; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_1_0_0; -.
DR InParanoid; Q8RDN5; -.
DR BioCyc; FNUC190304:G1FZS-2044-MONOMER; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000002521; 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..224
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179774"
FT HELIX 1..6
FT /evidence="ECO:0007829|PDB:5ZKN"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5ZKN"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:5ZKN"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:5ZKN"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:5ZKN"
SQ SEQUENCE 224 AA; 24823 MW; 9F47DE55E8924593 CRC64;
MNKILESIRG KLIVSCQALE DEPLHSSFIM GRMAYAAYSG GAAGIRANTV EDIKEIKKNV
SLPIIGIIKK VYNNSDVYIT PTIKEVEDLI NEGVQIIAID ATKRERPDRK DLKNFIAEIK
EKYPNQLFMA DISSVDEALY AEKIGFDIVG TTLVGYTDYT KNYKALEELK KVVKVVKIPV
IAEGNIDTPL KAKKALEIGA FAVVVGGAIT RPQQITKKFV DEMK
//
