ID   NANM1_ECOL6             Reviewed;         372 AA.
AC   Q8CVR2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=N-acetylneuraminate epimerase 1 {ECO:0000255|HAMAP-Rule:MF_01195};
DE            EC=5.1.3.24 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=N-acetylneuraminate mutarotase 1 {ECO:0000255|HAMAP-Rule:MF_01195};
DE            Short=Neu5Ac mutarotase 1 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=Sialic acid epimerase 1 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   Flags: Precursor;
GN   Name=nanM1 {ECO:0000255|HAMAP-Rule:MF_01195}; OrderedLocusNames=c3634;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN82082.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8CVR2; -.
DR   SMR; Q8CVR2; -.
DR   STRING; 199310.c3634; -.
DR   EnsemblBacteria; AAN82082; AAN82082; c3634.
DR   KEGG; ecc:c3634; -.
DR   eggNOG; COG3055; Bacteria.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; NCEAGSG; -.
DR   BioCyc; ECOL199310:C3634-MON; -.
DR   Proteomes; UP000001410; 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; Repeat;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           26..372
FT                   /note="N-acetylneuraminate epimerase 1"
FT                   /id="PRO_0000333057"
FT   REPEAT          44..88
FT                   /note="Kelch 1"
FT   REPEAT          90..141
FT                   /note="Kelch 2"
FT   REPEAT          143..177
FT                   /note="Kelch 3"
FT   REPEAT          178..223
FT                   /note="Kelch 4"
FT   REPEAT          226..269
FT                   /note="Kelch 5"
FT   REPEAT          291..340
FT                   /note="Kelch 6"
FT   REPEAT          342..371
FT                   /note="Kelch 7"
FT   ACT_SITE        232
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   372 AA;  40962 MW;  08D8C416CB8B5EFE CRC64;
     MITMKVKNFI YLPFCLFIGT SVAGALPEIP EPFKYGVGGI ENGKIYIGLG SLGNNWYMID
     TNQSEKKWTK IAQWPTVPRE QATATIIDGK IYVFGGIGKD TSGVITLQKD VYSYDIAKDK
     WEKLMTRPPV SLAGHVSFIH NGHAVSTGGV NENIFNGYFS DVELSKGNSA LTEKVNRDYF
     SKPADDYFLN NHIISYDPSK NQWKNLGTTP FPGTAGSSVI FAEQQIYILG GERKPGLRSV
     RSWTGELSHD RIKWSELPPV ASPEGVSGAY ASVIDGNIFL AGGAYFPGAA EKYSNGEYWS
     HKGLDKAYSK EIYQLIKNDW KKVGSLPEGL AYGVSLPWQG GMLILGGEKK DGKAVSDVIY
     LKKNDKQIKI VK