ID   NANM_SALNS              Reviewed;         386 AA.
AC   B4T2W1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
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};
GN   OrderedLocusNames=SNSL254_A1225;
OS   Salmonella newport (strain SL254).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=423368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL254;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001113; ACF64260.1; -; Genomic_DNA.
DR   RefSeq; WP_000525756.1; NZ_CCMR01000003.1.
DR   AlphaFoldDB; B4T2W1; -.
DR   SMR; B4T2W1; -.
DR   EnsemblBacteria; ACF64260; ACF64260; SNSL254_A1225.
DR   KEGG; see:SNSL254_A1225; -.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; PSTNKWR; -.
DR   Proteomes; UP000008824; 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; IPR019936; Mutatrotase_YjhT-like.
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..29
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           30..386
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_1000138425"
FT   REPEAT          51..95
FT                   /note="Kelch 1"
FT   REPEAT          97..149
FT                   /note="Kelch 2"
FT   REPEAT          151..186
FT                   /note="Kelch 3"
FT   REPEAT          187..232
FT                   /note="Kelch 4"
FT   REPEAT          235..284
FT                   /note="Kelch 5"
FT   REPEAT          306..355
FT                   /note="Kelch 6"
FT   REPEAT          357..386
FT                   /note="Kelch 7"
FT   ACT_SITE        241
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   386 AA;  42573 MW;  BFD37D669F11944F CRC64;
     MGMQMKNFKK MMTLMALCLS VAITTSGYAT TLPDIPEPLK NGTGAIDNNG VIYVGLGTAG
     TSWYKIDLKK QHKDWERIKS FPGGAREQSV SVFLNDELYV FGGVGKKNSE SPLQVYSDVY
     KYSPVKNTWQ KVDTISPVGL TGHTGVKLNE TMVLITGGVN EHIFDKYFID IAAAAADESE
     KNKVIYNYFN KPAKDYFFNK IVFIYNAKEN TWKNAGELPD AGTAGSSSVM ENNFLMLING
     ELKPGLRTDV IYRAMWDNDK LTWLKNSQLP PSPGEQQQEG LAGAFSGYSH GVLLVGGGAN
     FPGAKQNYTN GKFYSHEGIN KKWRDEVYGL VNGHWQYMGK MKQPLGYGVS VSYGDEVFLI
     GGENAKGKPV SSVTSFTMRD GNLLIK