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BSR_YERPE
ID   BSR_YERPE               Reviewed;         409 AA.
AC   Q8ZFL4; Q0WG98;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Broad specificity amino-acid racemase {ECO:0000255|HAMAP-Rule:MF_02212};
DE            EC=5.1.1.10 {ECO:0000255|HAMAP-Rule:MF_02212};
DE   Flags: Precursor;
GN   OrderedLocusNames=YPO1687, y1849, YP_1816;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC       substrates. {ECO:0000255|HAMAP-Rule:MF_02212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC         Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC         EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:32557; Evidence={ECO:0000255|HAMAP-Rule:MF_02212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02212};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02212};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_02212}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02212}.
CC   -!- CAUTION: The gene coding for this protein seems to be defective in
CC       strain 91001 where it is interrupted by the insertion of an IS285
CC       element. {ECO:0000305}.
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DR   EMBL; AL590842; CAL20330.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM85416.1; -; Genomic_DNA.
DR   EMBL; AE017042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; AG0205; AG0205.
DR   RefSeq; WP_002210868.1; NZ_WUCM01000082.1.
DR   RefSeq; YP_002346690.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZFL4; -.
DR   SMR; Q8ZFL4; -.
DR   STRING; 214092.YPO1687; -.
DR   PaxDb; Q8ZFL4; -.
DR   DNASU; 1146796; -.
DR   EnsemblBacteria; AAM85416; AAM85416; y1849.
DR   GeneID; 57976892; -.
DR   KEGG; ype:YPO1687; -.
DR   KEGG; ypk:y1849; -.
DR   PATRIC; fig|214092.21.peg.2032; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_6; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central.
DR   GO; GO:0047679; F:arginine racemase activity; IEA:RHEA.
DR   GO; GO:0018113; F:lysine racemase activity; IEA:RHEA.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR   CDD; cd06826; PLPDE_III_AR2; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_02212; Bsr_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR043698; Racemase_Bsr/Lyr.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Isomerase; Periplasm; Pyridoxal phosphate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   CHAIN           21..409
FT                   /note="Broad specificity amino-acid racemase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT                   /id="PRO_0000114603"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   MOD_RES         76
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   DISULFID        72..98
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
SQ   SEQUENCE   409 AA;  44770 MW;  BBFCC8C5A2E4241C CRC64;
     MHVRFRHLFL LPLITLVACS QPVSKNHLSL TSLSANAQQP VVNNAWLEIS QGALDFNTKK
     MLTLLDNKST LCAILKGDAY GHDLTLVTPV MLKNNVQCIG VASNQELKTV RDLGFTGQLI
     RVRSATLKEM QQAMAYDVEE LIGDKTVAEQ LNNIAKLNGK VLRIHLALNS AGMSRNGLEV
     SKARGLNDAK TIAGLKNLTI VGIMSHYPVE DASEIKADLA RFQQQAKDVI AVTGLKREKI
     KLHVANTFAT LAVPDSWLDM VRVGGVFYGD TIASTEYKRV MTFKSNIASL NNYPKGGTVG
     YDRTYTLKRD SLLANIPVGY ADGYRRVFSN AGHVIIQGQR LPVLGKTSMN TVIVDVTDLK
     KVSLGDEVVL FGKQGNAEIQ AEEIEDLSGA LFTEMSILWG ATNKRILVD
 
 
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