GSH1B_ORYSI
ID GSH1B_ORYSI Reviewed; 496 AA.
AC A2YL07;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 70.
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; ORFNames=OsI_025000;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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}.
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DR EMBL; CM000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A2YL07; -.
DR SMR; A2YL07; -.
DR STRING; 39946.A2YL07; -.
DR PRIDE; A2YL07; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000007015; Chromosome 7.
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_0000333023"
FT REGION 14..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 160..380
FT /evidence="ECO:0000250"
SQ SEQUENCE 496 AA; 56153 MW; F363C07A82631A7C 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
RKFRAGLALQ PIATAIFANS PFKEGKPNGY LSLRSHIWTD TDNNRSGMLP FVFDDSFGFE
RYVDYALDVP MYFVYRNKKY IDCTGMSFRD FMVGKLPQAP GELPTLNDWE NHLTTIFPEV
RLKRYLEMRG ADGGPWRRLC ALPAFWVGLL YDEESLQSIS DMTSDWTNEE REMLRRKVPV
TGLKTPFRDG YVRDLAEEIL QLSKNGLERR GYKEVSFLRE VDAVISSGVT PAERLLNLYE
TKWQRSVDPV FQELLY
