ID   GSH1_PSEA7              Reviewed;         527 AA.
AC   A6VDX9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=PSPA7_5948;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR82588.1; -; Genomic_DNA.
DR   RefSeq; WP_012077830.1; NC_009656.1.
DR   AlphaFoldDB; A6VDX9; -.
DR   SMR; A6VDX9; -.
DR   EnsemblBacteria; ABR82588; ABR82588; PSPA7_5948.
DR   KEGG; pap:PSPA7_5948; -.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001582; 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..527
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000025177"
SQ   SEQUENCE   527 AA;  59170 MW;  CEB29613D20B594C CRC64;
     MSDLLSRRLA LLGAAANLPL LTECLHGIER ECLRVDSDGK LALTPHPRAL GSTLTHPQIT
     TDYSEALLEF ITPTETDVAD TLGDLERIHR FASSQLDGEY LWSPSMPCEL PDEESIPIAR
     YGNSMIGRLK YVYRKGLALR YGKTMQCIAG IHYNFSLPEK LWPLLRQAEG SELAERDYQS
     AAYIALIRNF RRYSWLLMYL FGASPALDAG FLRGRPSQLE RFDEHTLYLP YATSLRMSDL
     GYQNNAQAGL TPCYNDLQSY IDSLRKAVST PYPAYEKIGT KQDGEWVQLN TNVLQIENEY
     YSSIRPKRVT YTGERPVQAL AARGVQYVEV RCLDINPFLP LGIDLDEARF LDAFLLFCAF
     SDSPLLNGEC SDATDNFLAV VKEGRRPGLQ LRRRGQPVEL KDWASELLER IADTAALLDR
     ARGGEAHAAA LAAQRAKVAD PELTPSAQVL KVMRERGESF EAFSLRQSRE HAEYFRQHPL
     AADEQARFEQ MASASLAEQA ELERDQDGDF DTFVAAYQAS ILGLISN