RBL_ORYSI
ID RBL_ORYSI Reviewed; 477 AA.
AC P0C511; P12089; Q6QY04; Q6QY68;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39;
DE Flags: Precursor;
GN Name=rbcL; ORFNames=9311063;
OS Oryza sativa subsp. indica (Rice).
OG Plastid; Chloroplast.
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=15122023; DOI=10.1104/pp.103.031245;
RA Tang J., Xia H., Cao M., Zhang X., Zeng W., Hu S., Tong W., Wang J.,
RA Wang J., Yu J., Yang H., Zhu L.;
RT "A comparison of rice chloroplast genomes.";
RL Plant Physiol. 135:412-420(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=cv. CO43; TISSUE=Leaf;
RX PubMed=20034395; DOI=10.1186/1477-5956-7-47;
RA Kandasamy S., Loganathan K., Muthuraj R., Duraisamy S., Seetharaman S.,
RA Thiruvengadam R., Ponnusamy B., Ramasamy S.;
RT "Understanding the molecular basis of plant growth promotional effect of
RT Pseudomonas fluorescens on rice through protein profiling.";
RL Proteome Sci. 7:47-47(2009).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC ChEBI:CHEBI:58272; EC=4.1.1.39;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC ChEBI:CHEBI:58272;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: Up-regulated in the leaf sheaths of rice plants grown from
CC seeds that were inoculated with the nonpathogenic P.fluorescens strain
CC KH-1. {ECO:0000269|PubMed:20034395}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=53418; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20034395};
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel' (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS46061.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY522329; AAS46061.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_009161372.1; NC_027678.1.
DR RefSeq; YP_654221.1; NC_008155.1.
DR AlphaFoldDB; P0C511; -.
DR SMR; P0C511; -.
DR STRING; 39946.P0C511; -.
DR PRIDE; P0C511; -.
DR GeneID; 4126887; -.
DR Proteomes; UP000007015; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IC:Gramene.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR CDD; cd08212; RuBisCO_large_I; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR InterPro; IPR020888; RuBisCO_lsuI.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Disulfide bond; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW Oxidoreductase; Photorespiration; Photosynthesis; Plastid;
KW Reference proteome.
FT PROPEP 1..2
FT /evidence="ECO:0000250"
FT /id="PRO_0000290099"
FT CHAIN 3..477
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000290100"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 3
FT /note="N-acetylproline"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 52881 MW; 8EECF4F8F1F0A8F9 CRC64;
MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV VGEDNQYIAY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL RALRLEDLRI PPTYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKSQA ETGEIKGHYL
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE MTLGFVDLLR DDFIEKDRAR
GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAAAN
RVALEACVQA RNEGRDLARE GNEIIRSACK WSPELAAACE IWKAIKFEFE PVDKLDS
