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Database: UniProt
Entry: A0A286GG83_9PROT
LinkDB: A0A286GG83_9PROT
Original site: A0A286GG83_9PROT 
ID   A0A286GG83_9PROT        Unreviewed;       458 AA.
AC   A0A286GG83;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=SAMN05421508_10414 {ECO:0000313|EMBL:SOD94531.1};
OS   Caenispirillum bisanense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Caenispirillum.
OX   NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD94531.1, ECO:0000313|Proteomes:UP000219621};
RN   [1] {ECO:0000313|EMBL:SOD94531.1, ECO:0000313|Proteomes:UP000219621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 140 {ECO:0000313|EMBL:SOD94531.1,
RC   ECO:0000313|Proteomes:UP000219621};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OCNJ01000004; SOD94531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286GG83; -.
DR   OrthoDB; 9780152at2; -.
DR   Proteomes; UP000219621; 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:SOD94531.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000219621};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DISULFID        116..336
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ   SEQUENCE   458 AA;  51117 MW;  8DEB4D25A953FB79 CRC64;
     MSGPSKPNLQ PITGRDDLVA WLESGNKPQD QWRMGTEHEK FAYRLSDKTA LPYADPNGGP
     GIRDMLEGLQ AYGWQPVEEN GNVIAMTRDD GGSISLEPGG QLELSGAPLE TVHQTCTEVT
     THRKQVREVA EKLGVGLIGL GFAPTWRRED MHWMPKGRYA IMRNYMPKVG TLGLDMMLRT
     CTVQVNMDYA SEADMVKKFR VATALQPVAT ALWANSPFTE GKPNGWRSYR AHIWTDTDNN
     RAGLPEFAFE DGFGFERYVD YLLDVPMYFV ARDGRYIDVA GRSFRDFLEG KLPELPGETP
     TVGDWADHAS TAFPDVRLKK YMEMRGSDGG PWSRLCALPA FWGGLLYDSD ALDEAWHLVK
     DWTPEERRAL HAGVPVTALK TPFRSGTVQD LALDALRIAR AGLGRRGRLS ADGMDESGFL
     EPLQRIAESG MSPADELLDA YQNRWNGSLE PLWAAYAY
//
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