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RBL_ORYSJ
ID   RBL_ORYSJ               Reviewed;         477 AA.
AC   P0C512; 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 100.
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; OrderedLocusNames=LOC_Osp1g00420; ORFNames=Nip064;
OS   Oryza sativa subsp. japonica (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=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RA   Nishizawa Y., Hirai A.;
RT   "Nucleotide sequence and expression of the gene for the large subunit of
RT   rice ribulose 1,5-bisphosphate carboxylase.";
RL   Jpn. J. Genet. 62:389-395(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=2770692; DOI=10.1007/bf02464880;
RA   Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., Mori M.,
RA   Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., Kanno A.,
RA   Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.;
RT   "The complete sequence of the rice (Oryza sativa) chloroplast genome:
RT   intermolecular recombination between distinct tRNA genes accounts for a
RT   major plastid DNA inversion during the evolution of the cereals.";
RL   Mol. Gen. Genet. 217:185-194(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
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   [4]
RP   PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 41-48; 180-186 AND 320-327, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16758443; DOI=10.1002/pmic.200600043;
RA   Nozu Y., Tsugita A., Kamijo K.;
RT   "Proteomic analysis of rice leaf, stem and root tissues during growth
RT   course.";
RL   Proteomics 6:3665-3670(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF ACTIVATED HOLOENZYME IN COMPLEX
RP   WITH MAGNESIUM AND NADP; 6-PHOSPHOGLUCONATE OR TRANSITION-STATE ANALOG
RP   2-CABP, SUBUNIT, AND CARBOXYLATION AT LYS-201.
RC   STRAIN=cv. Notohikari; TISSUE=Leaf;
RX   PubMed=22609438; DOI=10.1016/j.jmb.2012.05.014;
RA   Matsumura H., Mizohata E., Ishida H., Kogami A., Ueno T., Makino A.,
RA   Inoue T., Yokota A., Mae T., Kai Y.;
RT   "Crystal structure of rice Rubisco and implications for activation induced
RT   by positive effectors NADPH and 6-phosphogluconate.";
RL   J. Mol. Biol. 422:75-86(2012).
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.
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         Evidence={ECO:0000269|PubMed:22609438};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:22609438};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains
CC       (PubMed:22609438); disulfide-linked. The disulfide link is formed
CC       within the large subunit homodimers. {ECO:0000269|PubMed:22609438}.
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 (By similarity). The
CC       disulfide bond reported in 1WDD may be the result of oxidation during
CC       crystallization. {ECO:0000250|UniProtKB:P11383}.
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   -!- MISCELLANEOUS: NADPH and 6-phosphogluconate function as positive
CC       effectors to promote enzyme activation. {ECO:0000305|PubMed:22609438}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS46127.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D00207; BAA00147.1; -; Genomic_DNA.
DR   EMBL; X15901; CAA34004.1; -; Genomic_DNA.
DR   EMBL; AY522330; AAS46127.1; ALT_INIT; Genomic_DNA.
DR   PIR; JQ0231; RKRZL.
DR   RefSeq; NP_039391.1; NC_001320.1.
DR   RefSeq; YP_009305312.1; NC_031333.1.
DR   PDB; 1WDD; X-ray; 1.35 A; A/E=1-477.
DR   PDB; 3AXK; X-ray; 1.90 A; A/B=1-477.
DR   PDB; 3AXM; X-ray; 1.65 A; A/B/C/D/E/F/G/H=1-477.
DR   PDBsum; 1WDD; -.
DR   PDBsum; 3AXK; -.
DR   PDBsum; 3AXM; -.
DR   AlphaFoldDB; P0C512; -.
DR   SMR; P0C512; -.
DR   STRING; 4530.OS10T0356000-00; -.
DR   PaxDb; P0C512; -.
DR   PRIDE; P0C512; -.
DR   GeneID; 29141378; -.
DR   GeneID; 3131463; -.
DR   KEGG; osa:3131463; -.
DR   eggNOG; ENOG502QTI9; Eukaryota.
DR   InParanoid; P0C512; -.
DR   OrthoDB; 474428at2759; -.
DR   BRENDA; 4.1.1.39; 4460.
DR   EvolutionaryTrace; P0C512; -.
DR   PRO; PR:P0C512; -.
DR   Proteomes; UP000059680; Chloroplast.
DR   Genevisible; P0C512; OS.
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:0000166; F:nucleotide binding; 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; NADP; Nucleotide-binding; Oxidoreductase;
KW   Photorespiration; Photosynthesis; Plastid; Reference proteome.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000290101"
FT   CHAIN           3..477
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000290102"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         60
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:3AXK"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD"
FT   BINDING         68
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:3AXK"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXM"
FT   BINDING         127
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:3AXK"
FT   BINDING         173..177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD"
FT   BINDING         175
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:3AXK"
FT   BINDING         201..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXK,
FT                   ECO:0007744|PDB:3AXM"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXK,
FT                   ECO:0007744|PDB:3AXM"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD, ECO:0007744|PDB:3AXK,
FT                   ECO:0007744|PDB:3AXM"
FT   BINDING         294..295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0007744|PDB:1WDD"
FT   BINDING         295..298
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:3AXK"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0007744|PDB:1WDD"
FT   BINDING         379..381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:1WDD"
FT   BINDING         381
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:22609438,
FT                   ECO:0007744|PDB:3AXK"
FT   BINDING         404..405
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:22609438"
FT   SITE            334
FT                   /note="Transition state stabilizer"
FT   MOD_RES         3
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         201
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000269|PubMed:22609438"
FT   DISULFID        247
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000250"
FT   HELIX           21..24
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:3AXK"
FT   STRAND          97..103
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           113..121
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          130..139
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           155..162
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           182..194
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          207..209
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           214..232
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           247..260
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          263..268
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           274..287
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           298..302
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          305..309
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           311..321
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          324..327
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          331..335
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           339..350
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          375..381
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           384..386
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           387..394
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   STRAND          396..401
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           404..407
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           413..432
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           437..449
FT                   /evidence="ECO:0007829|PDB:1WDD"
FT   HELIX           453..462
FT                   /evidence="ECO:0007829|PDB:1WDD"
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
 
 
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