ID   NANE_STRSV              Reviewed;         232 AA.
AC   A3CK30;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=SSA_0071;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN43535.1; -; Genomic_DNA.
DR   RefSeq; WP_011836315.1; NC_009009.1.
DR   RefSeq; YP_001034085.1; NC_009009.1.
DR   AlphaFoldDB; A3CK30; -.
DR   SMR; A3CK30; -.
DR   STRING; 388919.SSA_0071; -.
DR   EnsemblBacteria; ABN43535; ABN43535; SSA_0071.
DR   KEGG; ssa:SSA_0071; -.
DR   PATRIC; fig|388919.9.peg.67; -.
DR   eggNOG; COG3010; Bacteria.
DR   HOGENOM; CLU_086300_1_0_9; -.
DR   OMA; QALGFDC; -.
DR   OrthoDB; 1710586at2; -.
DR   UniPathway; UPA00629; UER00682.
DR   Proteomes; UP000002148; 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; Reference proteome.
FT   CHAIN           1..232
FT                   /note="Putative N-acetylmannosamine-6-phosphate 2-
FT                   epimerase"
FT                   /id="PRO_0000301496"
SQ   SEQUENCE   232 AA;  25219 MW;  AF21C7BDC0D54AB6 CRC64;
     MSQILKDDLI AKIKDGIIVS CQALPQEPLY TEAGGVIPLL VKAAEQGGAV GIRANSVRDI
     REIKEVTSLP IIGIIKRDYP PQEPFITATM REVDELAALD IEVIALDCTK RERHDGLTVA
     DFIKQVKVKY PHQLLMADIS TYEEAAAAVE AGVDFVGTTL SGYTSYSPKV DGPDIELIRR
     LCQAGFDVIA EGKIHYPSQA KQIHDLGVRG IVVGGAITRP KEITERFVAG LK