GSH1_PSEU2
ID GSH1_PSEU2 Reviewed; 535 AA.
AC Q4ZZU4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
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}; OrderedLocusNames=Psyr_0255;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
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DR EMBL; CP000075; AAY35328.1; -; Genomic_DNA.
DR RefSeq; YP_233366.1; NC_007005.1.
DR AlphaFoldDB; Q4ZZU4; -.
DR SMR; Q4ZZU4; -.
DR STRING; 205918.Psyr_0255; -.
DR EnsemblBacteria; AAY35328; AAY35328; Psyr_0255.
DR KEGG; psb:Psyr_0255; -.
DR PATRIC; fig|205918.7.peg.254; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000426; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
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.
FT CHAIN 1..535
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025183"
SQ SEQUENCE 535 AA; 60446 MW; C87C32B725A2F56B CRC64;
MKDYTLSEFL NRRLALLGER NNLSLLEQCL HGIERECLRV TATAELACTP HPQALGAALT
NGQVTTDYSE SLLEFITPAL KNPAETIDNL DRIHRFVYSK LGDELLWSPS MPCPLPDEEH
IPIAYYGTSN IGKLKYVYRK GLALRYGKTM QCIAGIHYNF SLPEDAWALL KQTEDFAGDA
RDYQSHSYIA LIRNFRRYSW LLMYLFGASP ALDAGFLRGR KHQLEQHFDA DTLYLPYATS
LRMSDLGYQS DAQADLTPCY NDLVSYTDSL RKAVATPYKP YVEVGTHDQN GEWVQLNTNV
LQIENEYYSN IRPKRVTYSG ERPIQALVAR GVQYVEVRCL DINPFLPTGI SLEQSRFIDA
FVLYCALEES QQLARHECSN ASSNFLSVVK EGRRPGLSLM RDNRPVDLKT WATELMEKIT
PIARLLDQAQ GIDEHLKSIA VQQAKIDDTA LTPSAQVLAS MEAHNEGFTA FSLRQSQVHA
EYFRTHPLSA QEQADFEAQA KTSIEEQAEL EATEEVVDFD TFVGSYQASI LSISN
