NANE_VIBC3
ID NANE_VIBC3 Reviewed; 240 AA.
AC A5F7B9; C3M1H5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=VC0395_A1378, VC395_1895;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ20468.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP09891.1; -; Genomic_DNA.
DR RefSeq; WP_012034277.1; NZ_CP045719.1.
DR AlphaFoldDB; A5F7B9; -.
DR SMR; A5F7B9; -.
DR STRING; 345073.VC395_1895; -.
DR EnsemblBacteria; ABQ20468; ABQ20468; VC0395_A1378.
DR KEGG; vco:VC0395_A1378; -.
DR KEGG; vcr:VC395_1895; -.
DR PATRIC; fig|345073.21.peg.1835; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_0_0_6; -.
DR OMA; TRPMEIT; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000249; Chromosome 2.
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:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04729; NanE; 1.
DR Gene3D; 3.20.20.70; -; 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; PTHR36204; 1.
DR Pfam; PF04131; NanE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase.
FT CHAIN 1..240
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_1000073170"
SQ SEQUENCE 240 AA; 25530 MW; 72D2EC11476EA84F CRC64;
MRPVVRKNFL NIEELKRFLN GQTVVSIQPV TGSPLDKTDF IVAMAIAVEQ AGAKALRIEG
VNNVAAVSAA VTIPIIGIVK RDLPDSPIRI TPFVSDVDGL ANAGATVIAF DATDRTRPES
RERIAQAIKN TGCFAMADCS TFEDGLWANS QGVEIVGSTL SGYVGDIEPT VPDFQLVKAF
SEAGFFTMAE GRYNTPELAA KAIESGAVAV TVGSALTRLE VVTQWFNNAT QVAGERKCAH
