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GALM_SHIFL
ID   GALM_SHIFL              Reviewed;         346 AA.
AC   P0A9C4; P40681;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Aldose 1-epimerase;
DE            EC=5.1.3.3;
DE   AltName: Full=Galactose mutarotase;
DE   AltName: Full=Type-1 mutarotase;
GN   Name=galM; OrderedLocusNames=SF0548, S0556;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC       active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC       lactose (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC         ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10126};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN42192.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16065.1; -; Genomic_DNA.
DR   RefSeq; NP_706485.1; NC_004337.2.
DR   RefSeq; WP_000931389.1; NZ_UIQL01000012.1.
DR   AlphaFoldDB; P0A9C4; -.
DR   SMR; P0A9C4; -.
DR   STRING; 198214.SF0548; -.
DR   EnsemblBacteria; AAN42192; AAN42192; SF0548.
DR   EnsemblBacteria; AAP16065; AAP16065; S0556.
DR   GeneID; 1023468; -.
DR   GeneID; 66670973; -.
DR   KEGG; sfl:SF0548; -.
DR   KEGG; sfx:S0556; -.
DR   PATRIC; fig|198214.7.peg.637; -.
DR   HOGENOM; CLU_031753_1_0_6; -.
DR   OMA; ATWLSCK; -.
DR   OrthoDB; 1512477at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR013458; Ald_epimerase_bac.
DR   InterPro; IPR015443; Aldose_1-epimerase.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF005096; GALM; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   TIGRFAMs; TIGR02636; galM_Leloir; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..346
FT                   /note="Aldose 1-epimerase"
FT                   /id="PRO_0000197444"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10126"
FT   ACT_SITE        309
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  38190 MW;  4373732BAEA83E1D CRC64;
     MLNETPALAP DGQPYRLLTL RNNAGMVVTL MDWGATLLSA RIPLSDGSVR EALLGCASPE
     CYQDQAAFLG ASIGRYANRI ANSRYTFDGE TVTLSPSQGV NQLHGGPEGF DKRRWQIVNQ
     NDRQVLFALS SDDGDQGFPG NLGATVQYRL TDDNRISITY RATVDKPCPV NMTNHVYFNL
     DGEQSDVRNH KLQILADEYL PVDEGGIPHD GLKSVAGTSF DFRSAKIIAS EFLADDDQRK
     VKGYDHAFLL QAKGDGKKVA AHVWSADEKL QLKVYTTAPA LQFYSGNFLG GTPSRGTEPY
     ADWQGLALES EFLPDSPNHP EWPQPDCFLR PGEEYSSLTE YQFIAE
 
 
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