ID   NANM_SALAR              Reviewed;         386 AA.
AC   A9MH34;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=SARI_01870;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000880; ABX21753.1; -; Genomic_DNA.
DR   RefSeq; WP_012210278.1; NC_010067.1.
DR   AlphaFoldDB; A9MH34; -.
DR   SMR; A9MH34; -.
DR   STRING; 41514.SARI_01870; -.
DR   EnsemblBacteria; ABX21753; ABX21753; SARI_01870.
DR   KEGG; ses:SARI_01870; -.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; PSTNKWR; -.
DR   OrthoDB; 1977684at2; -.
DR   Proteomes; UP000002084; 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   SUPFAM; SSF117281; SSF117281; 2.
DR   TIGRFAMs; TIGR03547; muta_rot_YjhT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Kelch repeat; Periplasm;
KW   Reference proteome; Repeat; 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_0000333064"
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;  42234 MW;  CD357CFA29638B83 CRC64;
     MGMQMKNSKK MMTLMALCLS VAITTSGYAT TLPDIPEPLK NGTGAIDNNG VIYVGLGSAG
     TSWYKIDLKK QHKDWERIKS FPGGAREQSV SVFLNGELYV FGGVGKESNE APLQVYSDVY
     KYTPAKNTWQ KVNTISPVGL TGHTVVKLNE TMALITGGVN EHIFDKYFID IAAAAGDDSE
     KNRVIYNYFN KPSKDYFFNK IVFIYNAKEN TWENAGELPG AGTAGSSSAM ENNSLTLING
     ELKPGLRTDV IYRAIWDNDK LTWLKNSQLP PSPGEQHQEG LAGAFSGYSQ GVLLVGGGAN
     FPGAKQNYTD GKFYAHEGIN KKWRDEVYGL INGHWQYVGK MKQPLGYGVS VNYGDEIFLI
     GGENAKGKPV SSVISFAMHD GKLLIE