ID   NANM_PASMU              Reviewed;         380 AA.
AC   Q9CKB7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 117.
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=PM1707;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03791.1; -; Genomic_DNA.
DR   RefSeq; WP_005724596.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKB7; -.
DR   SMR; Q9CKB7; -.
DR   STRING; 747.DR93_654; -.
DR   EnsemblBacteria; AAK03791; AAK03791; PM1707.
DR   KEGG; pmu:PM1707; -.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; PSTNKWR; -.
DR   Proteomes; UP000000809; 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; 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..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           22..380
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_0000016657"
FT   REPEAT          42..86
FT                   /note="Kelch 1"
FT   REPEAT          88..140
FT                   /note="Kelch 2"
FT   REPEAT          142..176
FT                   /note="Kelch 3"
FT   REPEAT          177..222
FT                   /note="Kelch 4"
FT   REPEAT          225..274
FT                   /note="Kelch 5"
FT   REPEAT          296..349
FT                   /note="Kelch 6"
FT   REPEAT          351..380
FT                   /note="Kelch 7"
FT   ACT_SITE        231
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   380 AA;  40259 MW;  17AAFD265B585BB1 CRC64;
     MKFTKTALFT VLAATAFAAQ AGQYPDLPEG IKAGAGALIG DTVYVGLGGT GTTKFYSLNL
     KDPKEWKEIA EFPGGKRNQP VAAGVNGKLY VFGGFQDTDV AKNQIINDAY EYNPADNTWT
     KLSTRSPRST SVGASVAADG GKIYFVGGVN HEIWNGLFQD VKAAGGDKEK EKAIFDPYFN
     LRAQDFFFSP EIISYEPANN VWRNEGYFPY SGRAGAAVAI KDGKLLVVNG EVKAGLRSPG
     TALGTIGKDG VTWKKLGDLP APTGYDKQDG IAGGMGGYTN GHYIVTGGAN FPGALANYEK
     GIMDAHRTGG LKKTYHKAVY ALDGKTGNWK IVGELPATIG YGLAVSYNNK VLLIGGETDG
     GKPLSAVQTM SYDGKKLTVE