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RBL_ONYJA
ID   RBL_ONYJA               Reviewed;         414 AA.
AC   Q36610;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
DE   Flags: Fragment;
GN   Name=rbcL;
OS   Onychium japonicum (Japanese claw fern) (Carrot fern).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC   Pteridoideae; Onychium.
OX   NCBI_TaxID=32172;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   PubMed=8202555; DOI=10.1073/pnas.91.12.5730;
RA   Hasebe M., Omori T., Nakazawa M., Sano T., Kato M., Iwatsuki K.;
RT   "rbcL gene sequences provide evidence for the evolutionary lineages of
RT   leptosporangiate ferns.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5730-5734(1994).
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}.
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DR   EMBL; U05641; AAA19990.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q36610; -.
DR   SMR; Q36610; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.110; -; 1.
DR   Gene3D; 3.30.70.150; -; 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   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   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Disulfide bond; Lyase;
KW   Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid.
FT   CHAIN           <1..>414
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062551"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            312
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         179
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT   DISULFID        225
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         414
SQ   SEQUENCE   414 AA;  45729 MW;  DC857F2FCAEEB4AF CRC64;
     TYYTPEYQTK DTDILAAFRM TPQPGVPAEE AGAAVAAESS TGTWTTVWTD GLTSLDRYKG
     RCYDIEPVAG EENQYIAYVA YPLDLFEEGS VTNMLTSIVG NVFGFKALRA LRLEDLRIPP
     AYSKTFIGPP HGIQVERDKL NKYGRPLLGC TIKPKLGLSA KNYGRAVYEC LRGGLDFTKD
     DENVNSQPFM RWRDRFLFVA EALFKAQAET GEIKGHYLNA TAGTCEEMMK RAVFARELGA
     PIVMHDYLTG GFTANTSLAY YCRDNGLLLH IHRAMHAVID RQRNHGIHFR VLAKALRMSG
     GDHIHAGTVV GKLEGEREVT LGFVDLLRDD YIEKDRSRGI YFTQDWVSMP GVLPVASGGI
     HVWHMPALTE IFGDDSVLQF GGGTLGHPWG NAPGAVANRV ASEACVQALN EGLR
 
 
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