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6PGL_YERPE
ID   6PGL_YERPE              Reviewed;         334 AA.
AC   Q8ZGX4; Q0WHQ0; Q74W78; Q7CH64;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=6-phosphogluconolactonase {ECO:0000255|HAMAP-Rule:MF_01605};
DE            Short=6-P-gluconolactonase {ECO:0000255|HAMAP-Rule:MF_01605};
DE            EC=3.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01605};
GN   Name=pgl {ECO:0000255|HAMAP-Rule:MF_01605};
GN   OrderedLocusNames=YPO1149, y3033, YP_1011;
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: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-
CC       phosphogluconate. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC         + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01605};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       2/3. {ECO:0000255|HAMAP-Rule:MF_01605}.
CC   -!- SIMILARITY: Belongs to the cycloisomerase 2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01605}.
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DR   EMBL; AL590842; CAL19813.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM86584.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS61262.1; -; Genomic_DNA.
DR   PIR; AC0141; AC0141.
DR   RefSeq; WP_002210760.1; NZ_WUCM01000016.1.
DR   RefSeq; YP_002346188.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZGX4; -.
DR   SMR; Q8ZGX4; -.
DR   IntAct; Q8ZGX4; 7.
DR   STRING; 214092.YPO1149; -.
DR   PaxDb; Q8ZGX4; -.
DR   DNASU; 1147980; -.
DR   EnsemblBacteria; AAM86584; AAM86584; y3033.
DR   EnsemblBacteria; AAS61262; AAS61262; YP_1011.
DR   GeneID; 57977288; -.
DR   KEGG; ype:YPO1149; -.
DR   KEGG; ypk:y3033; -.
DR   KEGG; ypm:YP_1011; -.
DR   PATRIC; fig|214092.21.peg.1444; -.
DR   eggNOG; COG2706; Bacteria.
DR   HOGENOM; CLU_038716_2_0_6; -.
DR   OMA; EGNWPRD; -.
DR   UniPathway; UPA00115; UER00409.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_01605; 6P_gluconolactonase; 1.
DR   InterPro; IPR022528; 6-phosphogluconolactonase_YbhE.
DR   InterPro; IPR019405; Lactonase_7-beta_prop.
DR   InterPro; IPR011045; N2O_reductase_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF10282; Lactonase; 1.
DR   SUPFAM; SSF50974; SSF50974; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; Hydrolase; Reference proteome.
FT   CHAIN           1..334
FT                   /note="6-phosphogluconolactonase"
FT                   /id="PRO_0000171142"
SQ   SEQUENCE   334 AA;  36446 MW;  4BDAC511EF8E0F06 CRC64;
     MKQAVYVASP DSQQIHVWQL DSAGELTLLQ TVDVPGQVQP MAISPNQRHL YVGVRPDFGI
     VSYHIADDGT LTAAGMAPLP GSPTHIDTDR QGRFLFSASY SFNCVSISPI DTHGVVQAPI
     QQLDDLPAPH SANIDPTNQI LLVPCLKEDK VRLFDLSAEG QLTPHAQADI TVAAGAGPRH
     MAFHPNHQVA YCVNELNSSV DVYQISNNGQ EYHLVQSLDA MPADFTGTRW AADIHITPNG
     RYLYISDRTA NLLGIFTVSE DGRVISLVGH HLTEAQPRGF NIDHSGNFLI ASGQKSDHIE
     VYRIDQNTGE LTTLKRYPVG KGPMWVSIRG AQNS
 
 
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