RBL_WHEAT
ID RBL_WHEAT Reviewed; 477 AA.
AC P11383; Q7YKX2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 148.
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;
OS Triticum aestivum (Wheat).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Terachi T., Ogihara Y., Tsunewaki K.;
RT "The molecular basis of genetic diversity among cytoplasms of Triticum and
RT Aegilops. VI. Complete nucleotide sequences of the rbcL genes encoding
RT H- and L-type rubisco large subunits in common Wheat and Ae. crassa 4x.";
RL Jpn. J. Genet. 62:375-387(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Niu J.S.;
RT "Wheat chloroplast gene rbcL.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RA Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT sequence and contig clones.";
RL Plant Mol. Biol. Rep. 18:243-253(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-477.
RC STRAIN=cv. Chinese Spring; TISSUE=Seedling;
RX PubMed=1752425; DOI=10.1093/genetics/129.3.873;
RA Ogihara Y., Terachi T., Sasakuma T.;
RT "Molecular analysis of the hot spot region related to length mutations in
RT wheat chloroplast DNAs. I. Nucleotide divergence of genes and intergenic
RT spacer regions located in the hot spot region.";
RL Genetics 129:873-884(1991).
RN [5]
RP PROTEIN SEQUENCE OF 3-21, FUNCTION, ACETYLATION AT PRO-3, AND LACK OF
RP METHYLATION.
RX PubMed=2928307; DOI=10.1073/pnas.86.6.1855;
RA Houtz R.L., Stults J.T., Mulligan R.M., Tolbert N.E.;
RT "Post-translational modifications in the large subunit of ribulose
RT bisphosphate carboxylase/oxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1855-1859(1989).
RN [6]
RP DISULFIDE BOND.
RX PubMed=1733975; DOI=10.1016/S0021-9258(18)45951-0;
RA Mehta R.A., Fawcett T.W., Porath D., Mattoo A.K.;
RT "Oxidative stress causes rapid membrane translocation and in vivo
RT degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase.";
RL J. Biol. Chem. 267:2810-2816(1992).
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 (PubMed:2928307). Both
CC reactions occur simultaneously and in competition at the same active
CC site. {ECO:0000269|PubMed:2928307}.
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;
CC Note=Binds 1 Mg(2+) ion per subunit.;
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. {ECO:0000269|PubMed:1733975}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- PTM: The disulfide bond which can form between Cys-247 in the large
CC chain dimeric partners within the hexadecamer appears to be associated
CC with oxidative stress and protein turnover.
CC {ECO:0000269|PubMed:1733975}.
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'.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000305}.
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DR EMBL; D00206; BAA00146.1; -; Genomic_DNA.
DR EMBL; AY328025; AAP92166.1; -; mRNA.
DR EMBL; AB042240; BAB47042.1; -; Genomic_DNA.
DR EMBL; X62117; CAA44027.1; -; Genomic_DNA.
DR PIR; B32395; RKWTLC.
DR RefSeq; NP_114267.1; NC_002762.1.
DR PDB; 5WSK; X-ray; 1.78 A; A/B/C/D=1-477.
DR PDBsum; 5WSK; -.
DR AlphaFoldDB; P11383; -.
DR SMR; P11383; -.
DR STRING; 4565.EPlTAEP00000010047; -.
DR iPTMnet; P11383; -.
DR PRIDE; P11383; -.
DR GeneID; 803091; -.
DR KEGG; taes:803091; -.
DR eggNOG; ENOG502QTI9; Eukaryota.
DR HOGENOM; CLU_031450_2_0_1; -.
DR Proteomes; UP000019116; Chloroplast.
DR ExpressionAtlas; P11383; baseline.
DR Genevisible; P11383; TA.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; Direct protein sequencing; Disulfide bond; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid; Reference proteome.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:2928307"
FT /id="PRO_0000031447"
FT CHAIN 3..477
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000031448"
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 14
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:2928307"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 3
FT /note="N-acetylproline"
FT /evidence="ECO:0000269|PubMed:2928307"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000269|PubMed:1733975"
FT CONFLICT 144
FT /note="Y -> C (in Ref. 2; AAP92166)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="A -> R (in Ref. 4; CAA44027)"
FT /evidence="ECO:0000305"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:5WSK"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 214..232
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:5WSK"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 413..433
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:5WSK"
FT HELIX 453..461
FT /evidence="ECO:0007829|PDB:5WSK"
SQ SEQUENCE 477 AA; 52851 MW; F4B6FD91D792C001 CRC64;
MSPQTETKAG VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVSPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEDSQWICY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL RALRLEDLRI PPTYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKSQA ETGEIKGHYL
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE MTLGFVDLLR DDFIEKDRAR
GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAAAN
RVALEACVQA RNEGRDLARE GNEIIRAACK WSPELAAACE VWKAIKFEFE PVDTIDK
