GSH1_PSEE4
ID GSH1_PSEE4 Reviewed; 530 AA.
AC Q1IGL1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, 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=PSEEN0224;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK13191.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1IGL1; -.
DR SMR; Q1IGL1; -.
DR STRING; 384676.PSEEN0224; -.
DR EnsemblBacteria; CAK13191; CAK13191; PSEEN0224.
DR KEGG; pen:PSEEN0224; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000658; 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..530
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025179"
SQ SEQUENCE 530 AA; 59677 MW; A97CA469B928CEAF CRC64;
MKESILSDLL NRRLSLLGAN LDLLKQCLHG IERECLRVTD DGRLAQTPHP EALGSALTNE
QITTDYSESL LEFITPALAD PAKVLDSLEE IHRFVYTKLG GEYLWSPSMP CALPAEEDIP
IAEYGSSNIG KLKHVYRKGL ALRYGRTMQC IAGIHYNFSL PEALWPLLRD AEGGEQNDRD
YQSSAYIALI RNFRRYSWLL MYLFGASPTL DKGFLRGRPH QLEELDEQTL YLPYATSLRM
SDLGYQSNAQ AGLTPCYNNL ASYTDSLRKA VGTPYPPYVE VGTHKDGEWV QLNTNILQIE
NEYYSNIRPK RVTYTGERPI QALMSRGVQY VEVRCLDINP FLPVGIDLPE ARFLDAFLLF
CALEESPQLD NGECGQCTDN FLTVVKEGRR PGLELRRDGQ PVALKAWATE LIERIGQLAG
LLDRAHGGNA HAKALETQQA KVDDPELTPS AQVLARMTEH DETFVQFSLR QSRLHAEAFR
EQPLPAERQQ AYETLARESL AEQSRLEQQE VGDFDLFVGA YQASILAISN
