ID A0A2A4I653_9SPHN Unreviewed; 457 AA.
AC A0A2A4I653;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN ORFNames=COA07_14270 {ECO:0000313|EMBL:PCG13656.1};
OS Sphingomonas adhaesiva.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=28212 {ECO:0000313|EMBL:PCG13656.1, ECO:0000313|Proteomes:UP000218323};
RN [1] {ECO:0000313|EMBL:PCG13656.1, ECO:0000313|Proteomes:UP000218323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7418 {ECO:0000313|EMBL:PCG13656.1,
RC ECO:0000313|Proteomes:UP000218323};
RA Feng G., Zhu H.;
RT "Sphingomonas adhaesiva DSM 7418, whole genome shotgun sequence.";
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}.
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:PCG13656.1}.
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DR EMBL; NWVC01000007; PCG13656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4I653; -.
DR Proteomes; UP000218323; 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:PCG13656.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000218323};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DISULFID 114..334
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 457 AA; 50120 MW; 710887F04560936A CRC64;
MTTKTVSDSN AAVIESRDQL IAHFAGGEKP ADRWRIGTEH EKFVYSTTDH HAPSWGEPGG
IRALLLELVQ HGWTPVEEGG NIIALTGADG SVSLEPAGQF ELSGAPLDNL HQTCAETGRH
LQQVKAAGEK LGIGFLGLGM WPDKARDALP IMPKGRYAIM LRHMPRVGTM GLDMMLRTCT
IQVNLDYASE ADMAKKFRVG LALQPLATAL FANSPFTEGR PNGFLSYRSH IWSDTDPART
GMLPFVFEDG FGYERYADYM LDVPMYFVYR EGRYIDAAGL SFRDFLKGEL SVLPGEKPTM
DDWNDHLSTA FPEVRLKTFL EMRGADGGPW GRICALPALW VGLLYDQGAL DAAWDVVKDW
TLDERQALRD AVPKLGLDAP IAGGRRLRDV AGQVLDIAHA GLAARARTNA AGDDETGFLA
PLHEIVRSGK VPAQALLDRY NGAWDGDVSR VYGEESF
//
