ID A0A3L6R9T9_PANMI Unreviewed; 496 AA.
AC A0A3L6R9T9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN ORFNames=C2845_PM06G08190 {ECO:0000313|EMBL:RLM99626.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM99626.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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, ECO:0000256|PIRNR:PIRNR017901}.
CC -!- SIMILARITY: Belongs to the carboxylate-amine ligase family.
CC Glutamate--cysteine ligase type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010253, 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:RLM99626.1}.
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DR EMBL; PQIB02000009; RLM99626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6R9T9; -.
DR STRING; 4540.A0A3L6R9T9; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000275267; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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, ECO:0000256|PIRNR:PIRNR017901};
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};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 160..380
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 496 AA; 56221 MW; 501D3BAEF948B8A5 CRC64;
MAVASRLAVS RVSPDGAGPA AAPRRGRPAG FAAVGLPGRG RRRGGAVAAS PPMEEAVQMT
EPLTKEDLVA YLVSGCKPKE NWRIGTEHEK FGFEVDTLRP IKYDQIRDIL NGLAERFDWD
KIMEENNVIG LKQGKQSISL EPGGQFELSG APLETLHQTC AEVNSHLYQV KAVGEEMGIG
FLGLGFQPKW ALSDIPIMPK GRYEIMRNYM PKVGTLGLDM MFRTCTVQVN LDFSSEQDMI
RKFRAGLALQ PIATAIFANS PFKEGKPNGF LSLRSHIWTD TDNNRAGMLP FVFDDSFGFE
QYVDYALDVP MYFVYRNKKY IDCTGMSFRD FMQGKLPQAP GELPTLNDWE NHLTTIFPEV
RLKRYLEMRG ADGGPWRRLC ALPAFWVGLL YDEESLQSIL DMTFDWTKEE REMLRRKVPV
TGFKTPFRDG YVRDLAEEVL KLAKNGLERR GYKEVGFLRE VEETVGTGVT PAERLLNLYE
TKWQRNVDHV FEHLLY
//
