ID A0A418WAR4_9PROT Unreviewed; 453 AA.
AC A0A418WAR4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN ORFNames=D3874_08445 {ECO:0000313|EMBL:RJF87048.1};
OS Oleomonas cavernae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Oleomonas.
OX NCBI_TaxID=2320859 {ECO:0000313|EMBL:RJF87048.1, ECO:0000313|Proteomes:UP000284605};
RN [1] {ECO:0000313|EMBL:RJF87048.1, ECO:0000313|Proteomes:UP000284605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1W22B-8 {ECO:0000313|EMBL:RJF87048.1,
RC ECO:0000313|Proteomes:UP000284605};
RA Zhu H.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC).
CC {ECO:0000256|PIRNR:PIRNR017901}.
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:0000256|PIRNR:PIRNR017901};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000256|ARBA:ARBA00005006}.
CC -!- SUBUNIT: Homodimer or monomer when oxidized or reduced, respectively.
CC {ECO:0000256|ARBA:ARBA00011153}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the carboxylate-amine ligase family.
CC Glutamate--cysteine ligase type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010253}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC EgtA subfamily. {ECO:0000256|PIRNR:PIRNR017901}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJF87048.1}.
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DR EMBL; QYUK01000011; RJF87048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418WAR4; -.
DR OrthoDB; 9780152at2; -.
DR Proteomes; UP000284605; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.590.20; -; 1.
DR InterPro; IPR035434; GCL_bact_plant.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011556; Glut_cys_lig_pln_type.
DR NCBIfam; TIGR01436; glu_cys_lig_pln; 1.
DR PANTHER; PTHR34378; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR34378:SF1; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF04107; GCS2; 1.
DR PIRSF; PIRSF017901; GCL; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR017901-50};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Ligase {ECO:0000256|PIRNR:PIRNR017901, ECO:0000313|EMBL:RJF87048.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000284605};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DISULFID 111..331
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 453 AA; 50238 MW; 0BDCC91EC49FE60D CRC64;
MSGVQAAGEP IEDRRQLVEW MAEGGKPKAD YRIGTEHEKF GFRLDDLGPV PYDGPAGIRA
MLEGLRRFGW GPIYEGEHII ALEQNGASIS LEPGGQFELS GAPLETVHGT CGEVGTHLEQ
VRAVAGELGL GFLGLGFSPL WKRDEVPIMP KGRYDIMRSY MPKRGKLGLD MMLRTSTVQV
NLDFSNEADM VRKMCAAIAL QPVATALFAN SPFTEGKPNG YQSYRAHIWS DTDPDRTGMI
PFVFDQGFGF ERYVDWALDV PMYFVYRDGR YIDASGQSFR DFLAGRLPAL PGEKPHLGDW
SAHLTTLFPE ARLKRYIEMR GADGGPWNRL CALPALWVGL IYADDSLAAA LDLVKDWSAE
ERDALRAGVP RLALKTPFRK GSVLDVAREV VGIAEHGLKQ RAADNGMGSD ETMFLDILKR
TVDSGRTPAD DLLEAYHGRW NGDLTHLFKE HAY
//
