GSH1_VIBC1
ID GSH1_VIBC1 Reviewed; 522 AA.
AC A7MZY1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=VIBHAR_03486;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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; CP000789; ABU72431.1; -; Genomic_DNA.
DR RefSeq; WP_012128888.1; NC_022269.1.
DR AlphaFoldDB; A7MZY1; -.
DR SMR; A7MZY1; -.
DR PRIDE; A7MZY1; -.
DR EnsemblBacteria; ABU72431; ABU72431; VIBHAR_03486.
DR KEGG; vha:VIBHAR_03486; -.
DR PATRIC; fig|338187.25.peg.2714; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000008152; Chromosome I.
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..522
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025192"
SQ SEQUENCE 522 AA; 59106 MW; 3AF2A34B17009645 CRC64;
MTDFAARLKQ VASNPEVFKQ FGRGVERETL RYRQDGHLAT TPHPEGLGSA FTNKWITTDF
SESLLEFITP VSHEIPELMG QLKDIHHFTQ TKMGEEKMWP LSMPCYVGSE DDIQLAQYGS
SNSAKMKTLY REGLKRRYGS LMQIISGVHF NFSFPESFWD ALHGEQDEEA RQDTKSDAYF
ALIRNYYRFG WMIPYFFGAS PALCGSFIQG RETDLPFEKI GGTLFLPKAT SLRLSDLGYT
NSAQSVLKIG FNSIDQYLDG LSDAIRRPSE EFAEIGVKVD GEYRQLNSNI LQIENELYAP
IRPKRVTKSG EKPSEALQRG GVEYIEVRSL DVNPFSAVGV SEEQVRFLDL FLTWAALSDS
DPMDNCELEC WRDNWNKVIV SGREKGLMLQ IGCQGERLSL QDWAHRVFAD LRQIAVEMDS
AAGGNAYQAV CDKLESWIDE PELTISGQLL ELTKEHGGLG KVGCALGMKF REENLAHSYE
QYSADAMETE VATSLEKQKQ AEQSDTLSFD DFLEDYFAYL KQ
