ID C6XGY1_LIBAP Unreviewed; 457 AA.
AC C6XGY1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN Name=gshA {ECO:0000313|EMBL:ACT57634.1};
GN OrderedLocusNames=CLIBASIA_05340 {ECO:0000313|EMBL:ACT57634.1};
OS Liberibacter asiaticus (strain psy62).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT57634.1, ECO:0000313|Proteomes:UP000002744};
RN [1] {ECO:0000313|EMBL:ACT57634.1, ECO:0000313|Proteomes:UP000002744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX PubMed=19589076; DOI=10.1094/MPMI-22-8-1011;
RA Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA Gottwald T.;
RT "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus
RT Liberibacter asiaticus' obtained through metagenomics.";
RL Mol. Plant Microbe Interact. 22:1011-1020(2009).
RN [2] {ECO:0000313|EMBL:ACT57634.1, ECO:0000313|Proteomes:UP000002744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX PubMed=21784907; DOI=10.1128/AEM.05111-11;
RA Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H., Duan Y.;
RT "Diversity and plasticity of the intracellular plant pathogen and insect
RT symbiont, 'Candidatus Liberibacter asiaticus', revealed by hyper variable
RT prophage genes with intragenic tandem repeats.";
RL Appl. Environ. Microbiol. 77:6663-6673(2011).
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; CP001677; ACT57634.1; -; Genomic_DNA.
DR RefSeq; WP_015452990.1; NC_012985.3.
DR AlphaFoldDB; C6XGY1; -.
DR STRING; 537021.CLIBASIA_05340; -.
DR GeneID; 66286613; -.
DR KEGG; las:CLIBASIA_05340; -.
DR eggNOG; COG3572; Bacteria.
DR HOGENOM; CLU_026610_1_0_5; -.
DR OrthoDB; 9780152at2; -.
DR Proteomes; UP000002744; Chromosome.
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 Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Ligase {ECO:0000256|PIRNR:PIRNR017901, ECO:0000313|EMBL:ACT57634.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
SQ SEQUENCE 457 AA; 52304 MW; 192231EE7350CE29 CRC64;
MTCNPLANTI VTSIDDLVQH IASGIKPQEE FRIGTEHESF IFSRADHRPL PYDGEKSIVT
ILQAIQKKLA WKEIMDKGNI IGLANPLSKA GISIEPGGQL ELSTTTLQNV HQIKGEILGY
IQILKEITQN LDLGILGMGF NPKWKLDEMP IMPKSRYVLM KKYMPQVGTH GLDMMFRTCT
TQVSLDFSSE HDMATKLRVS FKLQPLATAI FASSPFAEGR INGFQSWRSE IWRHTDSDRT
EILPFILRDN SNFEHYAQWA LDIPMYFILR KKEYYCCTDI TFRQFMNGAL KGRIKEWHPT
LEDWENHLST LFPAVRLRNC LEMRGADSGR LENIFAVAAF WTGILYDSSA LQNADHLTSS
WSFYDINKLN NTVPSKGMRS TVRGQSLKDI AIQILTFAHQ GLKNRSAKNH LQEDETIFLK
PLEKIIHNNQ TTADEMLAAY HTRWGKSIDP CFEEYAY
//
