ID A0A0N1C7P9_9SPHN Unreviewed; 457 AA.
AC A0A0N1C7P9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN ORFNames=IP81_09210 {ECO:0000313|EMBL:KPF92175.1};
OS Novosphingobium sp. AAP83.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523425 {ECO:0000313|EMBL:KPF92175.1, ECO:0000313|Proteomes:UP000037998};
RN [1] {ECO:0000313|EMBL:KPF92175.1, ECO:0000313|Proteomes:UP000037998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP83 {ECO:0000313|EMBL:KPF92175.1,
RC ECO:0000313|Proteomes:UP000037998};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF92175.1}.
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DR EMBL; LJHY01000016; KPF92175.1; -; Genomic_DNA.
DR RefSeq; WP_054107660.1; NZ_LJHY01000016.1.
DR AlphaFoldDB; A0A0N1C7P9; -.
DR STRING; 1523425.IP81_09210; -.
DR PATRIC; fig|1523425.4.peg.1029; -.
DR OrthoDB; 9780152at2; -.
DR Proteomes; UP000037998; 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:KPF92175.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000037998};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DISULFID 114..334
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 457 AA; 51007 MW; EBB398AEA090A4D3 CRC64;
MSTRQVSDRN DPIIENRDML VAPMQKGEKP AERWRIGTEH EKFVYRTQDR RAPSYTEQGG
IRDLLMAMTE FGWEPVLEGG NVIAMSGRDG AISLEPAGQL ELSGAPLENL HQTCAETGRH
LAQVKTIGDK LGLGYLGLGL WPDKTREELP IMPKGRYDIM LRHMPRVGSM GLDMMLRTCT
IQVNLDYSSE ADMVKKFRTS LALQPLATAL FANSPFLEGK PNGMLSYRSH IWTDTDPART
GMLSFVFDEG FGYERYVDYM LDVPMYFVYR DGKYIDASGL SFRDFLDGKL SVLPGEKPRA
SDWVDHLSTA FPEVRLKSFL EMRGADGGPW NRICALPALW VGLLYDQTAL DAAWDLVKDC
DMDGREKLRA EVPKLGLDAA LPGGGKLRDI AAEVLAISRS GLSARNRLNE AGDNETGYLQ
PLDEIIATGF TPAERLLNLY NGEWGGDLSR IYAEKSF
//
