GSH1_PSEPF
ID GSH1_PSEPF Reviewed; 532 AA.
AC Q3KJQ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=Pfl01_0257;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA72001.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3KJQ5; -.
DR SMR; Q3KJQ5; -.
DR STRING; 205922.Pfl01_0257; -.
DR PRIDE; Q3KJQ5; -.
DR EnsemblBacteria; ABA72001; ABA72001; Pfl01_0257.
DR KEGG; pfo:Pfl01_0257; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000002704; 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..532
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025182"
SQ SEQUENCE 532 AA; 59302 MW; 4A96C284BB0BC5F6 CRC64;
MKESKLSELL NRRLALLGER ANLSLLEQCL HGIERECLRV TGEGRLAQTP HPEALGSALT
NEQITTDYSE SLLEFITPAL PDPADTLASL DKIHRFAYSK LGNEYLWSPS MPCPLPAEED
IPIAYYGTSN IGQLKYVYRK GLALRYGKTM QCIAGIHYNF SLPEKLWPLL KEAEGFVGTD
RDFQSSSYIA LIRNFRRYSW LLMYLFGASP ALDAGFLRGR AHQLEQLDPD TLYLPYATSL
RMSDLGYQSN AQAGLTPCYN DLASYTDSLR KAVATPYAPY VEVGTHQDGE WVQLNTNILQ
IENEYYSNIR PKRVTYTGER PIQALMARGI QYVEVRCLDI NPFLPMGIDL TESRFLDAFL
LYCALNESPL LTNNSCGNAT SNFLSVVKEG RRPGLQLQRD GQPVELKEWA AELLEKIAPL
AALLDQSHGG DAHSKALDAQ LAKVKDSSLT PSAQVLAAMA AHKESFAQFS LRQSQAHAEF
FRSEPLAAEE QAKFEELARS SLAQQAELEQ NEVGDFDVFV GSYQASILAI SN