GSH1_YERPE
ID GSH1_YERPE Reviewed; 519 AA.
AC Q8ZBU2; Q0WBZ1;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578};
GN OrderedLocusNames=YPO3301, y0887, YP_0385;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00578};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00578}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM84471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS60658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL21892.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84471.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS60658.1; ALT_INIT; Genomic_DNA.
DR PIR; AI0400; AI0400.
DR RefSeq; WP_002228236.1; NZ_WUCL01000139.1.
DR RefSeq; YP_002348197.1; NC_003143.1.
DR AlphaFoldDB; Q8ZBU2; -.
DR SMR; Q8ZBU2; -.
DR STRING; 214092.YPO3301; -.
DR PaxDb; Q8ZBU2; -.
DR DNASU; 1145834; -.
DR EnsemblBacteria; AAM84471; AAM84471; y0887.
DR EnsemblBacteria; AAS60658; AAS60658; YP_0385.
DR KEGG; ype:YPO3301; -.
DR KEGG; ypk:y0887; -.
DR KEGG; ypm:YP_0385; -.
DR PATRIC; fig|214092.21.peg.3771; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0006750; P:glutathione biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_00578; Glu_cys_ligase; 1.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006334; Glut_cys_ligase.
DR PANTHER; PTHR38761; PTHR38761; 1.
DR Pfam; PF04262; Glu_cys_ligase; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..519
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192547"
SQ SEQUENCE 519 AA; 58471 MW; 3B639BF12E4286A2 CRC64;
MIPDVSHALT WLEAHPKALK GIRRGIERET LRVTADGHLA STGHPESLGA ALTHQWITTD
FAEALLEFIT PVDGDIDHLL TFLRDIHRYT ARKLGDERMW PLSMPCFIEA EQDIELAKYG
SSNIGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPLEFW QAWAGVTDEQ SGKEEISAGY
FRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GRETALPFER NGKGMCYLPY ATSLRLSDLG
YTNKSQSNLG ITFNDLHTYV DALKRAIQTP SEEYVALGLK DGDRHLQLNT NVLQIENELY
APIRPKRVTR AGESPSDALL RGGIEYIEVR SLDINPFSPI GVDAVQARFL DLFLIWCVLA
DAPEMSSDEL LCTRKNWDRV ILEGRKPGQT IGIGCSDSRQ PLETVGKALF ADLRRVAEVL
DGSESASYQQ VCDELVASFD DPELTFSARI LKVMQEKGSG GVGLELAEHY REMLQNEPLE
LLTEEQLSAE RDASRQRQHE LELKDKLSFE EYLALHGGQ
