ID   NANE_STRA3              Reviewed;         232 AA.
AC   P65518; Q8E2F5; Q8E7W3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=gbs0032;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(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; AL766843; CAD45677.1; -; Genomic_DNA.
DR   RefSeq; WP_001120330.1; NC_004368.1.
DR   AlphaFoldDB; P65518; -.
DR   SMR; P65518; -.
DR   STRING; 211110.gbs0032; -.
DR   EnsemblBacteria; CAD45677; CAD45677; CAD45677.
DR   KEGG; san:gbs0032; -.
DR   eggNOG; COG3010; Bacteria.
DR   HOGENOM; CLU_086300_1_0_9; -.
DR   OMA; QALGFDC; -.
DR   UniPathway; UPA00629; UER00682.
DR   Proteomes; UP000000823; Chromosome.
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..232
FT                   /note="Putative N-acetylmannosamine-6-phosphate 2-
FT                   epimerase"
FT                   /id="PRO_0000179803"
SQ   SEQUENCE   232 AA;  25196 MW;  D3A38BBC4A77F2C6 CRC64;
     MPHLSKEAFK KQIKNGIIVS CQALPGEPLY TESGGVMPLL ALAAQEAGAV GIRANSVRDI
     KEIQEVTNLP IIGIIKREYP PQEPFITATM TEVDQLASLD IAVIALDCTL RERHDGLSVV
     EFIQKIKRKY PEQLLMADIS TFEEGKNAFE AGVDFVGTTL SGYTDYSRQE EGPDIELLNK
     LCQAGIDVIA EGKIHTPKQA NEINHIGVAG IVVGGAITRP KEIAERFISG LS