GSH1_PSEAB
ID GSH1_PSEAB Reviewed; 527 AA.
AC Q02EG1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=PA14_68730;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ14587.1; -; Genomic_DNA.
DR RefSeq; WP_003141926.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02EG1; -.
DR SMR; Q02EG1; -.
DR PRIDE; Q02EG1; -.
DR EnsemblBacteria; ABJ14587; ABJ14587; PA14_68730.
DR KEGG; pau:PA14_68730; -.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR BioCyc; PAER208963:G1G74-5792-MON; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000653; 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_1000025178"
SQ SEQUENCE 527 AA; 59206 MW; 766ACA88D0C7C90E CRC64;
MSDLLSRRLA LLGAAANLPL LTECLHGIER ECLRVDSDGK LALTPHPRAL GSTLTHPQIT
TDYSEALLEF ITPTETDVAD TLGDLERIHR FASSKLDGEY LWSPSMPCEL PDEESIPIAR
YGSSLIGRLK YVYRKGLALR YGKTMQCIAG IHYNFSLPER LWPLLRQAEG SELSERDYQS
AAYIALIRNF RRYSWLLMYL FGASPALDAG FLRGRPSQLE RLDEHTLYLP YATSLRMSDL
GYQNNAQAGL TPCYNDLQSY IDSLRQAVST PYPPYEKVGT KQDGEWVQLN TNILQIENEY
YSSIRPKRVT YTGERPVQAL AARGVQYVEV RCLDINPFLP LGIDLDEARF LDAFLLFCAF
SDSPLLNGEC SDATDNFLAV VKEGRRPGLQ LQRRGQPVEL KVWANELLER IADTAALLDR
ARGGEAHAAA LAAQRAKVAD AELTPSAQVL KVMRERGESF EAFSLRQSRE HAEYFRQHPL
AAEEQARFEK MASDSLAEQT ELERDQDGDF DTFVAAYQAS ILGLISN
