NANM_SALTI
ID NANM_SALTI Reviewed; 384 AA.
AC Q8Z7N0; Q7C999;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=STY1167, t1790;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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; AE014613; AAO69412.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD08255.1; -; Genomic_DNA.
DR RefSeq; NP_455625.1; NC_003198.1.
DR RefSeq; WP_000525766.1; NZ_WSUR01000018.1.
DR AlphaFoldDB; Q8Z7N0; -.
DR SMR; Q8Z7N0; -.
DR STRING; 220341.16502302; -.
DR EnsemblBacteria; AAO69412; AAO69412; t1790.
DR KEGG; stt:t1790; -.
DR KEGG; sty:STY1167; -.
DR PATRIC; fig|220341.7.peg.1167; -.
DR eggNOG; COG3055; Bacteria.
DR HOGENOM; CLU_061535_0_0_6; -.
DR OMA; PSTNKWR; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT CHAIN 30..384
FT /note="N-acetylneuraminate epimerase"
FT /id="PRO_0000333067"
FT REPEAT 51..95
FT /note="Kelch 1"
FT REPEAT 97..149
FT /note="Kelch 2"
FT REPEAT 151..184
FT /note="Kelch 3"
FT REPEAT 185..230
FT /note="Kelch 4"
FT REPEAT 233..282
FT /note="Kelch 5"
FT REPEAT 304..353
FT /note="Kelch 6"
FT REPEAT 355..384
FT /note="Kelch 7"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ SEQUENCE 384 AA; 42386 MW; C26E48237F9B660B CRC64;
MGMQMKNFKK MMTLMALCLS VAITTSGYAT TLPDIPEPLK NGTGAIDNNG VIYVGLGTAG
TSWYKIDLKK QHKDWERIKS FPGGAREQSV SVFLNDKLYV FGGVGKKNSE SPLQVYSDVY
KYSPVKNTWQ KVDTISPVGL TGHTGVKLNE TMVLITGGVN EHIFDKYFID IAAADESEKN
KVIYNYFNKP AKDYFFNKIV FIYNAKENTW KNAGELPGAG TAGSSSVMEN NFLMLINGEL
KPGLRTDVIY RAMWDNDKLT WLKNSQLPPS PGEQQQEGLA GAFSGYSHGV LLVGGGANFP
GAKQNYTNGK FYSHEGINKK WRDEVYGLIN GHWQYMGKMK QPLGYGVSVS YGDEVFLIGG
ENAKGKPVSS VTSFTMRDGN LLIK
