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Entry: A0A239PV17_9PROT
LinkDB: A0A239PV17_9PROT
Original site: A0A239PV17_9PROT 
ID   A0A239PV17_9PROT        Unreviewed;       457 AA.
AC   A0A239PV17;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000256|PIRNR:PIRNR017901};
DE            EC=6.3.2.2 {ECO:0000256|PIRNR:PIRNR017901};
GN   ORFNames=SAMN06297382_2052 {ECO:0000313|EMBL:SNT74144.1};
OS   Amphiplicatus metriothermophilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Amphiplicatus.
OX   NCBI_TaxID=1519374 {ECO:0000313|EMBL:SNT74144.1, ECO:0000313|Proteomes:UP000198346};
RN   [1] {ECO:0000313|EMBL:SNT74144.1, ECO:0000313|Proteomes:UP000198346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12710 {ECO:0000313|EMBL:SNT74144.1,
RC   ECO:0000313|Proteomes:UP000198346};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-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}.
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DR   EMBL; FZQA01000004; SNT74144.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239PV17; -.
DR   OrthoDB; 9780152at2; -.
DR   Proteomes; UP000198346; 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:SNT74144.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR017901};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198346};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DISULFID        115..335
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017901-50"
SQ   SEQUENCE   457 AA;  50717 MW;  0A441D0B9C9F07F6 CRC64;
     MSTASPQEPG APPIESIDQL TAYLEAGSKP KSEWRIGTEH EKFVYCRTSL KPVGYEGETG
     IRAILEEMSR RSGWSLIVEN GLPIGLRGDG ATVSLEPGGQ FELSGAPLEN IHQTCEEVHA
     HLALVKDVAG PTGVSFFGMG FAPTWTLAEM PRMPKPRYDI MRRYMPKVGR LGLDMMHRTC
     TVQVNLDFSD EADMAAKFRV GLALQPIATA LFANSSLVEG KPVGWASWRA KVWTDTDPDR
     TGLLDFVFEP GFGFERYAEY ILDVPMYFVR RNGRYIDAAG QSFRDFLAGR LPALPGERPT
     IGDWEDHLST AFPEVRMKRF LEMRGADGGP WARICALPAF WVGLLYDETA LAAAWDIAKG
     WSREERERLR VDAAHYGLRA KIGSRTVQDV AKEALAIARE GLKRRARANW QGADESIFLD
     TFCEIAESGV TLGEATARRF VEELKGDARA LLAEASY
//
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