ID A0A1H3HWR6_9RHOB Unreviewed; 456 AA.
AC A0A1H3HWR6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN ORFNames=SAMN05444340_104203 {ECO:0000313|EMBL:SDY19705.1};
OS Citreimonas salinaria.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Citreimonas.
OX NCBI_TaxID=321339 {ECO:0000313|EMBL:SDY19705.1, ECO:0000313|Proteomes:UP000199286};
RN [1] {ECO:0000313|EMBL:SDY19705.1, ECO:0000313|Proteomes:UP000199286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26880 {ECO:0000313|EMBL:SDY19705.1,
RC ECO:0000313|Proteomes:UP000199286};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNPF01000004; SDY19705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3HWR6; -.
DR STRING; 321339.SAMN05444340_104203; -.
DR OrthoDB; 9780152at2; -.
DR Proteomes; UP000199286; 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:SDY19705.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000199286};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DISULFID 112..332
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 456 AA; 50493 MW; 162F0BCD4888A8C6 CRC64;
MSIPQSGGGP IERHEQLAEY LAAGCKPKDQ WRIGTEHEKF GYCKDSHRPL PYDGARSIKA
VLEGLRDRHG WSEVREGGKI IGLEKDGANV SLEPGGQLEL SGAPLETIHQ TCDEVNAHLA
DVKDIADEIG VGFIGLGAAP EWSHDDMPLM PKGRYALMDG YMQKVGTAGT TMMRRTCTVQ
VNLDFASEAD MVQKMRVALA LQPVATALFA NSPFFEGKPN GHKSWRARVW RHLDEARTGM
LPFAFDDGFG FEAWVDYVLD VPMYFVYRDG KYIDALGQSF RDFLKGELPA LPGEKPTLSD
WADHLTTVFP EARVKKFIEM RGADGGPWRR LCALPAFWVG LIYDQGALDA AWDLVKNWDA
ETREALRVAA SVDGLQAEVN GISMHALARE VLKIAEAGLK ARARPGAGGL VPDETHFLNA
LKESVESGEV PADELLRRYH GDWNGDLSRI YDEYSY
//
