NANM_ECO57
ID NANM_ECO57 Reviewed; 368 AA.
AC Q8X554; Q7A8N2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
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};
GN OrderedLocusNames=Z5906, ECs5269;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG59492.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB38692.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG59492.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB38692.1; ALT_INIT; Genomic_DNA.
DR PIR; E91287; E91287.
DR PIR; H86128; H86128.
DR RefSeq; NP_313296.1; NC_002695.1.
DR RefSeq; WP_001301833.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X554; -.
DR SMR; Q8X554; -.
DR STRING; 155864.EDL933_5643; -.
DR EnsemblBacteria; AAG59492; AAG59492; Z5906.
DR EnsemblBacteria; BAB38692; BAB38692; ECs_5269.
DR GeneID; 913698; -.
DR KEGG; ece:Z5906; -.
DR KEGG; ecs:ECs_5269; -.
DR PATRIC; fig|386585.9.peg.5503; -.
DR eggNOG; COG3055; Bacteria.
DR HOGENOM; CLU_061535_0_0_6; -.
DR OMA; PSTNKWR; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT CHAIN 20..368
FT /note="N-acetylneuraminate epimerase"
FT /id="PRO_0000333055"
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; 39550 MW; 4F1757CA0AFD5E3B CRC64;
MNKTITALAI LMASFAANAS VLPETPVPFK SGTGAIDNDT VYIGLGSAGT AWYKLETQAK
DKKWTALAAF PGGPRDQATS AFIDGNLYVF GGIGKNSEGL TQVFNDVHKY NPKTNSWVKL
ISHAPMGMAG HVTFVHNGKA YVTGGVNQNI FNGYFEDLNE AGKDSTAVDK INAHYFDKKA
EDYFFNKFLL SFDPSTQQWS YAGESPWYGT AGAAVVNKGD KTWLINGEAK PGLRTDAVFE
LDFTGNNLKW NRLAPVSSPD GVAGGFAGIS NDSLIFAGGA GFKGSRENYQ NGKNYAHEGL
KKSYSTDIHL WHNGKWDKSG ELSQGRAYGV SLPWNNSLLI IGGETAGGKA VTDSVLISVK
DNKVTVQN
