ID A0A2R8BJB7_9RHOB Unreviewed; 456 AA.
AC A0A2R8BJB7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN Name=egtA {ECO:0000313|EMBL:SPH23401.1};
GN ORFNames=DEA8626_02465 {ECO:0000313|EMBL:SPH23401.1};
OS Defluviimonas aquaemixtae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Defluviimonas.
OX NCBI_TaxID=1542388 {ECO:0000313|EMBL:SPH23401.1, ECO:0000313|Proteomes:UP000244924};
RN [1] {ECO:0000313|EMBL:SPH23401.1, ECO:0000313|Proteomes:UP000244924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8626 {ECO:0000313|EMBL:SPH23401.1,
RC ECO:0000313|Proteomes:UP000244924};
RA Keele B.F.;
RL Submitted (MAR-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}.
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DR EMBL; OMOQ01000002; SPH23401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8BJB7; -.
DR OrthoDB; 9780152at2; -.
DR Proteomes; UP000244924; 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:SPH23401.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000244924};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DISULFID 112..332
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 456 AA; 50873 MW; D8E92E1E98888287 CRC64;
MSIPQSGGGP IERFEQLAEY LEAGCKSVAD WRIGTEHEKF GFCKDTLKPL PYDGPRSIRA
MLEGLRDRYG WQAIEEQDNI IGLVKDGANV SLEPGGQLEL SGAPLETIHQ TCDEVNEHLR
EVQSVADDIG ARFIGLGAAP IWTHEDMPMM PKGRYRLMTD YMGRVGTHGT QMMYRTCTVQ
VNLDFSSEAD MVKKMRVALA LQPVATALFA NSPFFEGKPN GHKSWRSRIW RNLDDARTGM
LPFMFEDGAG FQRYVDYALD VPMYFVYRDG KYVDALGQSF RDFLKGELPA LPGEKPTLSD
WADHLTTIFP EARLKKFIEM RGADGGPWRR LCALPALWVG LLYDMSALDA AWDIAKGWDA
ETRSALRVAA SVDGLQAEAH GVKMRDVARN VLAVAEAGLK ARAKPGADGM IPDETHFLNA
LQESVESGNV PADELLEKYR GEWNGDLTRI YAEYSY
//
