ID   NANM_VIBVY              Reviewed;         384 AA.
AC   Q7MD39;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=VVA1197;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000038; BAC97223.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MD39; -.
DR   SMR; Q7MD39; -.
DR   STRING; 672.VV93_v1c41240; -.
DR   EnsemblBacteria; BAC97223; BAC97223; BAC97223.
DR   KEGG; vvy:VVA1197; -.
DR   eggNOG; COG3055; Bacteria.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; PSTNKWR; -.
DR   Proteomes; UP000002675; Chromosome II.
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; IPR011043; Gal_Oxase/kelch_b-propeller.
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; SSF50965; SSF50965; 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_0000333074"
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;  41511 MW;  67C29EA07FB62AE5 CRC64;
     MMKTKYLLLP LLASSSLLSH MAFANNHWPD LPIGVKNGVS AQIGSKVYVG LGSAEKSFYV
     LDTQAPQNGW TLLAEFIGPE RSGATATVVG ENIFVFGGSG KASDDASSPI IFDTVYRFDT
     QTNRWHQVKT QTPVGLLGAS SYSPDGKQVL FFGGYSKPLF DKYLADITRT DKKAQPEQWQ
     KIVDDYMGME PLAYQWNRDV LSFNPTNDKW DVVTRSPYLP NCGSATVIDG PSITLISGEI
     KPGLRTAEVK TFTYGELQPW QSTYALPAAK GQAQQEGIAG AYSGVVSNTL LVAGGANFHG
     AKAQFESGQM FAHNGLSKAY NSEIYAKQKG VWQQVGQLPE GLAYGASFSV KGGVLMVGGE
     RADRTASTKV YLVGLNNNQI DIVD