ID   NANE_YERPY              Reviewed;         233 AA.
AC   B1JFV9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=YPK_1401;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA67695.1; -; Genomic_DNA.
DR   RefSeq; WP_012303881.1; NC_010465.1.
DR   AlphaFoldDB; B1JFV9; -.
DR   SMR; B1JFV9; -.
DR   EnsemblBacteria; ACA67695; ACA67695; YPK_1401.
DR   KEGG; ypy:YPK_1401; -.
DR   PATRIC; fig|502800.11.peg.2039; -.
DR   OMA; TRPMEIT; -.
DR   UniPathway; UPA00629; UER00682.
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..233
FT                   /note="Putative N-acetylmannosamine-6-phosphate 2-
FT                   epimerase"
FT                   /id="PRO_1000139718"
SQ   SEQUENCE   233 AA;  24541 MW;  3AF146499B121001 CRC64;
     MSNLNNLRHK LQNGLIASCQ PVPGSAMDTP EIVAAMACAA LAGGAVGLRI EGINNIRAVR
     RATDAPIIGI IKRDLPDSEV RITPWLEDID ALSAAGADII AFDVTCRERP VSVADLYQRA
     RATGCLTMAD ASNIDDGLLA HHLGIDFIGT TLSGYTQATV PTEPDLALVT QLAQAGCRVI
     AEGRYHSPAL AAAAISAGAY AVTVGSAITR IEHICGWFCD AIKQCETEKL TEY