RBL_ORYSA
ID RBL_ORYSA Reviewed; 477 AA.
AC P0C510; 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 77.
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=PA064;
OS Oryza sativa (Rice).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4530;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PA64s;
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).
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 -!- 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 -!- 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=AAS46190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY522331; AAS46190.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_009305312.1; NC_031333.1.
DR PDB; 6KYI; X-ray; 1.75 A; A/B=1-477.
DR PDB; 6KYJ; X-ray; 1.70 A; A/C/E/G=1-477.
DR PDBsum; 6KYI; -.
DR PDBsum; 6KYJ; -.
DR AlphaFoldDB; P0C510; -.
DR SMR; P0C510; -.
DR IntAct; P0C510; 1.
DR PRIDE; P0C510; -.
DR GeneID; 29141378; -.
DR ExpressionAtlas; P0C510; baseline and differential.
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 3D-structure; Acetylation; Calvin cycle; Carbon dioxide fixation;
KW Chloroplast; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
FT PROPEP 1..2
FT /evidence="ECO:0000250"
FT /id="PRO_0000031329"
FT CHAIN 3..477
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000031330"
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"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:6KYJ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6KYI"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 214..232
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 336..350
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:6KYJ"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:6KYJ"
FT HELIX 453..461
FT /evidence="ECO:0007829|PDB:6KYJ"
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
