ID   NANM2_ECOL6             Reviewed;         368 AA.
AC   Q8CVG5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=N-acetylneuraminate epimerase 2 {ECO:0000255|HAMAP-Rule:MF_01195};
DE            EC=5.1.3.24 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=N-acetylneuraminate mutarotase 2 {ECO:0000255|HAMAP-Rule:MF_01195};
DE            Short=Neu5Ac mutarotase 2 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=Sialic acid epimerase 2 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   Flags: Precursor;
GN   Name=nanM2 {ECO:0000255|HAMAP-Rule:MF_01195}; OrderedLocusNames=c5388;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83810.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83810.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001304537.1; NC_004431.1.
DR   AlphaFoldDB; Q8CVG5; -.
DR   SMR; Q8CVG5; -.
DR   STRING; 199310.c5388; -.
DR   EnsemblBacteria; AAN83810; AAN83810; c5388.
DR   KEGG; ecc:c5388; -.
DR   eggNOG; COG3055; Bacteria.
DR   HOGENOM; CLU_061535_0_0_6; -.
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; IPR019936; Mutatrotase_YjhT-like.
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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           20..368
FT                   /note="N-acetylneuraminate epimerase 2"
FT                   /id="PRO_0000333058"
FT   REPEAT          40..84
FT                   /note="Kelch 1"
FT   REPEAT          86..137
FT                   /note="Kelch 2"
FT   REPEAT          139..173
FT                   /note="Kelch 3"
FT   REPEAT          174..219
FT                   /note="Kelch 4"
FT   REPEAT          222..265
FT                   /note="Kelch 5"
FT   REPEAT          287..336
FT                   /note="Kelch 6"
FT   REPEAT          338..367
FT                   /note="Kelch 7"
FT   ACT_SITE        228
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   368 AA;  39580 MW;  5039FF1091ED117F CRC64;
     MNKTITALAI LMASFAANAS VLPETPVPFK SGTGVIDNDT VYIGLGSAGT AWYKLDTQAK
     DKRWTALAAF PGGPRDQATS AFIDGNLYVF GGIGKNSEGL TQVFNDVHKY NPKTNSWVKL
     MSHAPMGMAG HVTFVHNGKA YVTGGVNQNI FNGYFEDLNE AGKDSTAIDK INAYYFDKKA
     EDYFFNKFLL SFDPSTQQWS YAGESPWYGT AGAAVVNKGD KTWLINGEAK PGLRTDAVFE
     LDFTGNNLKW NKLAPVASPD GVAGGFAGMS NDSLIFAGGA GFKGSRENYQ NGKNYAHEGL
     KKSYSADIHL WHNGKWDKSG ELSQGRAYGV SLLWNNSLLI IGGEAAGGKA VTDSVLISVK
     DNKVTVQN