GSH1_HAHCH
ID GSH1_HAHCH Reviewed; 525 AA.
AC Q2S8F7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, 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=HCH_06422;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC33067.1; -; Genomic_DNA.
DR RefSeq; WP_011400119.1; NC_007645.1.
DR AlphaFoldDB; Q2S8F7; -.
DR SMR; Q2S8F7; -.
DR STRING; 349521.HCH_06422; -.
DR EnsemblBacteria; ABC33067; ABC33067; HCH_06422.
DR KEGG; hch:HCH_06422; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000238; 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..525
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025173"
SQ SEQUENCE 525 AA; 59532 MW; 90E10169B68FCB67 CRC64;
MSEKLAARLE KLRRRHPQAL ADIYRGIEKE GLRVDSKGFI AQSDHPQALG SALTHPNITT
DYSEALLELI TPVTREVDEL LTSLQEIHQF VHANLPAGES LWAGSMPSLL DGDESIRIAE
YGESNLGKIK HVYRRGLAYR YGRIMQSIAG VHFNFSLGDD FWRAYQEVLA QSAPLQEFKS
ESYFSLIRNF RRWSWLLMYL FGASPALDRS FLNGRDHKLD QFGTDTLGLP HATSLRMSDL
GYQNNAQSSL KICFNHLSTY VKTLYDATHT PFPRYEAIGL QRDGEYIQLN ANLLQIENEY
YNTIRPKRVT QSGEKPIQAL KRRGIEYIEV RCLDLDPFSP IGVSESQIRF LDAFLLTCLL
SDSAKIVDEE CSIIEENFLT AVSRGRATDV ELVRLLQNDY VQGGLQEWAS RILEQVELCA
RELDAIKGGD SYAVAVRDAR AKVNDPSLTP SARTYAAVSN GQSYVDWTLA MSQAHHQTLI
ANPLSPERMQ HYVRAGEQSW ADERALREAD NLSFDAYLKQ YLTYV
