ID A0A2V0P8C6_9CHLO Unreviewed; 484 AA.
AC A0A2V0P8C6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 13-SEP-2023, 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=Rsub_07907 {ECO:0000313|EMBL:GBF95192.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF95192.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF95192.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF95192.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
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:GBF95192.1}.
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DR EMBL; BDRX01000061; GBF95192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V0P8C6; -.
DR STRING; 307507.A0A2V0P8C6; -.
DR InParanoid; A0A2V0P8C6; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000247498; Unassembled WGS sequence.
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:UP000247498};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 148..368
FT /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ SEQUENCE 484 AA; 54563 MW; 3B4B93F04254430E CRC64;
MAAGMPIRQE LGARAPGARP RQLGPRPAGP GLRQRVVCPA NAPQEGPAIP VNREDLIEHI
RSGCKPRDRW RIGTEHEKLG FRLADRRRMD YDEIRQVFEK LHSRFGWQPI KEGDLTIGAI
LDGQSVTLEP GGQFELSGAP VSTLHQTCAE VNSHLYQVKS IAEELGIGFL GAGFDPKWRI
EDIPVMPKDR YRLMKAYMPT VGKRGLDMMF RTCTIQVNLD FESERDMIEK FRIGLALQPV
AVALFANSPF AEGRPTGELS TRARVWMDVD RARTGGLPFV FDDDMSFERY VDYAMDVPMY
FVYRKGKYIN ALGMSWRDFM EGKLPALPGE RPTISDWENH LTTIFPDVRL KRYLEMRGAD
GGPWRLICAL PALWVGLLYD PQAQAEALDL IRGWSEDERE YLRSEVGIHG LATPFRGGTL
RDVALKVLDI SKGGLERRGH DEAAFLKSLQ LIAESGKTPA DALLELYNGK WGRSVDPIYD
ELAY
//
