GSH1_CLOAB
ID GSH1_CLOAB Reviewed; 481 AA.
AC Q97IV1;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=CA_C1539;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79506.1; -; Genomic_DNA.
DR PIR; G97089; G97089.
DR RefSeq; NP_348166.1; NC_003030.1.
DR RefSeq; WP_010964847.1; NC_003030.1.
DR AlphaFoldDB; Q97IV1; -.
DR SMR; Q97IV1; -.
DR STRING; 272562.CA_C1539; -.
DR EnsemblBacteria; AAK79506; AAK79506; CA_C1539.
DR GeneID; 44998038; -.
DR KEGG; cac:CA_C1539; -.
DR PATRIC; fig|272562.8.peg.1741; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_9; -.
DR OMA; REAMHEP; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000814; 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;
KW Reference proteome.
FT CHAIN 1..481
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192523"
SQ SEQUENCE 481 AA; 56715 MW; 68E9FA8B6C982442 CRC64;
MHWSFPEMIR LFSDEYRSSM LSEGNFGVER ESQRVNYSGD LALTPHPSVF GDKFENPRIT
TDFSESQIEM ITPPLKSAEE VYKALNDINN EVKNALKGEL LWPLSMPPRL PKEEDIPVAQ
FPDTEDGRQK QIYRNGLALR YGKKMQMISG IHYNFSFSDK MIDFIYRQLR IEKTKRQFID
EMYFSLTRNF LRYHWILIYL FGASPICDST YNSVIFKELE KIEKCCPHCA GKIKNFNRYA
TSLRVSRFGY SDTDEKKYTV YFNSLREYET KIKKMMETES NKYSKLGIYK DGVQIQLNGN
LLQSESEFYA PIRFKRNIKK GETQLTALVN RGVEYIEIRI LDVNPFDKVG ISVEQMNFLQ
VFNVFCLFEE SKSIDEEQME RINTNHQLAA LLGRNEDLML YKYNDDSRIP LKNFGDEIFE
KLRIVAKLMD KDNVEKKYSE SVESEYKKLH NIELLPSERI CREMDNDNRS YIQFGMEYAE
A