ID   NANM_VIBCH              Reviewed;         384 AA.
AC   Q9KR69;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=VC_1774;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF94923.1; -; Genomic_DNA.
DR   PIR; C82159; C82159.
DR   RefSeq; NP_231409.1; NC_002505.1.
DR   RefSeq; WP_001056548.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KR69; -.
DR   SMR; Q9KR69; -.
DR   STRING; 243277.VC_1774; -.
DR   DNASU; 2613654; -.
DR   EnsemblBacteria; AAF94923; AAF94923; VC_1774.
DR   GeneID; 57740418; -.
DR   KEGG; vch:VC_1774; -.
DR   PATRIC; fig|243277.26.peg.1694; -.
DR   eggNOG; COG3055; Bacteria.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; PSTNKWR; -.
DR   BioCyc; VCHO:VC1774-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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; 1.
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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           25..384
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_0000016658"
FT   REPEAT          46..90
FT                   /note="Kelch 1"
FT   REPEAT          92..145
FT                   /note="Kelch 2"
FT   REPEAT          147..184
FT                   /note="Kelch 3"
FT   REPEAT          185..230
FT                   /note="Kelch 4"
FT   REPEAT          233..281
FT                   /note="Kelch 5"
FT   REPEAT          303..352
FT                   /note="Kelch 6"
FT   REPEAT          354..383
FT                   /note="Kelch 7"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   384 AA;  41944 MW;  513B179249784BE6 CRC64;
     MNMKTLLTYA TLLSVTAFSH VVYADNQWPD LPTGFKDGVG AQVGSKVYVG LGSLGKSFYV
     LDLNALSKGW QKIADFTGAE RSGATASVIG NYIYLFGGSG KAEPSDPSPI LFDSVYRYDT
     KKDSWEKMNT TSPVGLLGAS SYSPDNRQIL FFGGYNKAYF DRYLRDISTT DKQVNPEVWQ
     RIVDDYMGMT PTDYKWNRNV ISYLPEKQEW RDLGVSTYLP NCGSATVIEG NKVTLISGEI
     KPGLRTAEVK QYEFGMDQPW KSLLPLPAPQ TSNIQEGVAG AFSGKTNGVV VVAGGANFHG
     AKQAFENGKM FAHEGLPKAF NSEIYVEKEG IWSTVNSLPE GLAYGASFTT SEGVLIVGGE
     KSGKEMSHKV YMLAWNGSTV EVID