GSH1_PSEPW
ID GSH1_PSEPW Reviewed; 525 AA.
AC B1JET4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=PputW619_4969;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) 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; CP000949; ACA75445.1; -; Genomic_DNA.
DR AlphaFoldDB; B1JET4; -.
DR SMR; B1JET4; -.
DR STRING; 390235.PputW619_4969; -.
DR EnsemblBacteria; ACA75445; ACA75445; PputW619_4969.
DR KEGG; ppw:PputW619_4969; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
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..525
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000129600"
SQ SEQUENCE 525 AA; 58932 MW; 0E7C0234D7B929C9 CRC64;
MSDLLNRRLS LLGANLPLLK QCLHGIEREC LRVTDEGRLA QTPHPESLGS ALTNEQITTD
YSESLLEFIT PALPDPAQVL ESLEQTHRFV YSKLGDELLW SPSMPCTLPA EEDIPIAEYG
ASNIGKLKHV YRKGLALRYG RTMQCIAGIH YNFSLPEALW PLLRASDGNE QSDRDYQSAA
YIALIRNFRR YSWLLMYLFG ASPALDKGFL RGRPHQLEEL DAETLYLPYA TSLRMSDLGY
QSNAQAGLTP CYNNLASYTD SLRKAVGTPY PPYVEIGTHV DGEWVQLNTN ILQIENEYYS
NIRPKRVTYT GERPIQALTS RGVQYVEVRC LDINPFLPVG IDLTEARFLD AFLLFCALED
SPLLDNGECG QCTDNFLTVV KEGRRPGLEL RRDGHPIELK AWASDLLGRI GQLAELLDRA
QGGDEHAKAL AAQQAKVDDA SLTPSAQVLA RMGEHEESFI QFSLRQSRLH AETFREQPLP
TERQQAYETL ARNSLAEQSR LEQEEVGDFD LFVGAYQASI LAISN
