ID   GSH1B_ORYSJ             Reviewed;         496 AA.
AC   Q6Z3A3; A3BJG6; Q0D6N0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glutamate--cysteine ligase B, chloroplastic;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-ECS B;
DE            Short=GCS B;
DE   AltName: Full=Gamma-glutamylcysteine synthetase B;
DE   Flags: Precursor;
GN   Name=GSH1-2; OrderedLocusNames=Os07g0462000, LOC_Os07g27790;
GN   ORFNames=P0038F09.39;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2.
CC   -!- SUBUNIT: Homodimer or monomer when oxidized or reduced, respectively.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- PTM: The Cys-160-Cys-380 disulfide bridge is known to modulate the
CC       enzyme activity according to the redox status. The oxidized form
CC       constitutes the active enzyme (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the carboxylate-amine ligase family. Glutamate--
CC       cysteine ligase type 2 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF21493.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP005256; BAC84166.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAF21493.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015647910.1; XM_015792424.1.
DR   AlphaFoldDB; Q6Z3A3; -.
DR   SMR; Q6Z3A3; -.
DR   STRING; 39947.Q6Z3A3; -.
DR   PaxDb; Q6Z3A3; -.
DR   PRIDE; Q6Z3A3; -.
DR   GeneID; 4343165; -.
DR   KEGG; osa:4343165; -.
DR   InParanoid; Q6Z3A3; -.
DR   OrthoDB; 397529at2759; -.
DR   PlantReactome; R-OSA-1119342; Gamma-glutamyl cycle.
DR   PlantReactome; R-OSA-1119483; Glutathione biosynthesis.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   Genevisible; Q6Z3A3; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
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   PANTHER; PTHR34378; PTHR34378; 1.
DR   PANTHER; PTHR34378:SF1; PTHR34378:SF1; 1.
DR   Pfam; PF04107; GCS2; 1.
DR   PIRSF; PIRSF017901; GCL; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01436; glu_cys_lig_pln; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Disulfide bond; Glutathione biosynthesis; Ligase;
KW   Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..496
FT                   /note="Glutamate--cysteine ligase B, chloroplastic"
FT                   /id="PRO_0000333024"
FT   REGION          14..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        160..380
FT                   /evidence="ECO:0000250"
FT   CONFLICT        63
FT                   /note="L -> F (in Ref. 4; CM000144)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   496 AA;  56153 MW;  A232857B83631A75 CRC64;
     MAVASRLAVA RVAPDGGAAG RRRRRRGRPV VAVPTAAGRG RGRGGAVAAS PPTEEAVQMT
     EPLTKEDLMA YLVSGCKPKE NWRIGTEHEK FGFEVDTLRP IKYDQIRDIL NGLAERFDWD
     KIVEENNVIG LKQGKQSISL EPGGQFELSG APLETLHQTC AEVNSHLYQV KAVGEEMGIG
     FLGIGFQPKW ALSDIPIMPK GRYEIMRNYM PKVGSLGLDM MFRTCTVQVN LDFSSEQDMI
     RKFRTGLALQ PIATAIFANS PFKEGKPNGY LSLRSHIWTD TDNNRSGMLP FVFDDSFGFE
     RYVDYALDVP MYFVYRNKKY IDCTGMSFRD FMVGKLPQAP GELPTLNDWE NHLTTIFPEV
     RLKRYLEMRG ADGGPWRRLC ALPAFWVGLL YDEESLQSIS DMTSDWTNEE REMLRRKVPV
     TGLKTPFRDG YVRDLAEEIL QLSKNGLERR GYKEVGFLRE VDAVISSGVT PAERLLNLYE
     TKWQRSVDPV FQELLY