GSH1_ENT38
ID GSH1_ENT38 Reviewed; 514 AA.
AC A4WDQ2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Ent638_3168;
OS Enterobacter sp. (strain 638).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=399742;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638;
RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA Vangronsveld J., Newman L., Monchy S.;
RT "Genome sequence of the plant growth promoting endophytic bacterium
RT Enterobacter sp. 638.";
RL PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP61832.1; -; Genomic_DNA.
DR RefSeq; WP_015960162.1; NC_009436.1.
DR AlphaFoldDB; A4WDQ2; -.
DR SMR; A4WDQ2; -.
DR STRING; 399742.Ent638_3168; -.
DR EnsemblBacteria; ABP61832; ABP61832; Ent638_3168.
DR KEGG; ent:Ent638_3168; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000230; 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..514
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000061182"
SQ SEQUENCE 514 AA; 57975 MW; 41642E636E026858 CRC64;
MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGSLA TTGHPESLGS ALTHKWITTD
FAEALLEFIT PVDGDIDHML TLMRDVHRYT ARQLGDERMW PLSMPCYIEQ GQDIELAQYG
TSNIGRLKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGETDKE AISAGYFRLI
RNYYRFGWVI PYLFGASPAI CSSFLQGKPT TLPFEKTDCG MYYLPYATSL RLSDLGYTNK
SQSNLGITFN DLHEYVAGLK RAIKTPSEEY ETIGLEKDGK RLQINSNVLQ IENELYAPIR
PKRVTRSGEA PSDALERGGI EYIEVRSLDI NPFSPIGVDE QQIRFLDLFM VWCVLADAPE
MSSDELLCTR TNWNRVILEG RKPGLTLGIG CETAQFPLAK VGKDLFRDLK RVAQTMDSLY
GGEEYQKVCD QLVESFDNPE LTFSARILRS MIDQGIGGTG RTLAAQYRDM LQQEPLEVLS
EEDFVAEREA SIARQREVEA GDTESFEAFL AKHA
