ID   NANM_YERE8              Reviewed;         392 AA.
AC   A1JMV0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=N-acetylneuraminate epimerase {ECO:0000255|HAMAP-Rule:MF_01195};
DE            EC=5.1.3.24 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=N-acetylneuraminate mutarotase {ECO:0000255|HAMAP-Rule:MF_01195};
DE            Short=Neu5Ac mutarotase {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=Sialic acid epimerase {ECO:0000255|HAMAP-Rule:MF_01195};
DE   Flags: Precursor;
GN   Name=nanM {ECO:0000255|HAMAP-Rule:MF_01195}; OrderedLocusNames=YE1943;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-
CC       anomer, accelerating the equilibrium between the alpha- and beta-
CC       anomers. Probably facilitates sialidase-negative bacteria to compete
CC       sucessfully for limited amounts of extracellular Neu5Ac, which is
CC       likely taken up in the beta-anomer. In addition, the rapid removal of
CC       sialic acid from solution might be advantageous to the bacterium to
CC       damp down host responses. {ECO:0000255|HAMAP-Rule:MF_01195}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminate;
CC         Xref=Rhea:RHEA:25233, ChEBI:CHEBI:58705, ChEBI:CHEBI:58770;
CC         EC=5.1.3.24; Evidence={ECO:0000255|HAMAP-Rule:MF_01195};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01195}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01195}.
CC   -!- SIMILARITY: Belongs to the NanM family. {ECO:0000255|HAMAP-
CC       Rule:MF_01195}.
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DR   EMBL; AM286415; CAL12022.1; -; Genomic_DNA.
DR   RefSeq; WP_011816245.1; NC_008800.1.
DR   RefSeq; YP_001006198.1; NC_008800.1.
DR   AlphaFoldDB; A1JMV0; -.
DR   SMR; A1JMV0; -.
DR   STRING; 393305.YE1943; -.
DR   EnsemblBacteria; CAL12022; CAL12022; YE1943.
DR   KEGG; yen:YE1943; -.
DR   PATRIC; fig|393305.7.peg.2100; -.
DR   eggNOG; COG3055; Bacteria.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; PSTNKWR; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; -; 2.
DR   HAMAP; MF_01195; NanM; 1.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR019936; Mutatrotase_YjhT-like.
DR   Pfam; PF01344; Kelch_1; 1.
DR   SMART; SM00612; Kelch; 1.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   TIGRFAMs; TIGR03547; muta_rot_YjhT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Kelch repeat; Periplasm; Repeat;
KW   Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           36..392
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_5000201151"
FT   REPEAT          56..100
FT                   /note="Kelch 1"
FT   REPEAT          102..155
FT                   /note="Kelch 2"
FT   REPEAT          157..192
FT                   /note="Kelch 3"
FT   REPEAT          193..238
FT                   /note="Kelch 4"
FT   REPEAT          241..290
FT                   /note="Kelch 5"
FT   REPEAT          312..361
FT                   /note="Kelch 6"
FT   REPEAT          363..392
FT                   /note="Kelch 7"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   392 AA;  42265 MW;  C8117DE20D3E0B6B CRC64;
     MTQIYHQYKK KLSTKVILLS ALTLCITFSL PYANAERYPD VPVAFKYGTG ARVDNHLYVG
     LGSAGQSWYR LDTDKASSGW QKIADFPGQP REQAVTVALS GKLYVFGGVG KNSASDTQVR
     ALDDVYQYDP QTNQWQRLAT RAPRGLVGTA ATTLNGTQAL LLGGVNKAIF DGYFTDLAAA
     GGNETQKNAV VNAYFDQAPA DYFYNRDVLM YDPAKNQWKS GGQVPFLGTA GSAITAKKGD
     LILINGEIKP GLRTAAVWQG KTQGTELKWQ QRPDLIGAEK GAVQEGLAGA FAGVSHDVVL
     VGGGANFPGS WQQFNAGQLY AHQGLKKQWQ QPIYALVDNQ WQVAGKLPQP LAYGVSIQDK
     DKVILLGGET SDGVATSAVT QLSWQGGKLH LE