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Database: UniProt
Entry: A0A1G8LBY2_9RHOB
LinkDB: A0A1G8LBY2_9RHOB
Original site: A0A1G8LBY2_9RHOB 
ID   A0A1G8LBY2_9RHOB        Unreviewed;       456 AA.
AC   A0A1G8LBY2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE            EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN   ORFNames=SAMN04487993_100675 {ECO:0000313|EMBL:SDI53155.1};
OS   Salipiger marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=555512 {ECO:0000313|EMBL:SDI53155.1, ECO:0000313|Proteomes:UP000199093};
RN   [1] {ECO:0000313|EMBL:SDI53155.1, ECO:0000313|Proteomes:UP000199093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26424 {ECO:0000313|EMBL:SDI53155.1,
RC   ECO:0000313|Proteomes:UP000199093};
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; FNEJ01000006; SDI53155.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8LBY2; -.
DR   STRING; 555512.SAMN04487993_100675; -.
DR   OrthoDB; 9780152at2; -.
DR   Proteomes; UP000199093; 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:SDI53155.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199093};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DISULFID        112..332
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ   SEQUENCE   456 AA;  50043 MW;  7D65511F2B861AE7 CRC64;
     MSIPQTGGGP IEHQTQLAEY LASGCKPKSD WRIGTEHEKF GYLTDTHAPL PYEGPRSILA
     VLEGLRDRFG WAEVREAGKL IGLTKGDANV SLEPGGALEL SGAPLETIHQ TCDEVNEHLR
     EVKGIADEIG VGFIGLGAAP EWHHDDMPLM PKGRYKLMDS YMGKVGTLGR VMMRRTCTVQ
     VNLDFGSEAD MVQKLRVALA LQPVATALFA NSPFFEGKPN GMKSFRGAVW RDLDGARTGM
     LPFVFEDGFG FERYVDYALD VPMYFVYRNG EYIDALGQSF RDFLKGELPA LPGEMPTLSD
     WADHLTTIFP EARLKKFIEM RGADGGPWRR LCALPALWVG LTYDQGALDA AWDLVKGWDA
     QTRDALRVAA STDGLQAQVG NINMHDLARE VLAIAEAGLT SRACPGAGGL LPDETHFLNA
     LKESVDSGKT AADELLEHYH GDWQGDLSRI YGAYSY
//
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