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RBL_OLILU
ID   RBL_OLILU               Reviewed;         488 AA.
AC   P14959;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE            Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE            EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
GN   Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS   Olisthodiscus luteus (Marine phytoflagellate).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Olisthodiscophyceae;
OC   Olisthodiscaceae; Olisthodiscus.
OX   NCBI_TaxID=83000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1536932; DOI=10.1007/bf00040676;
RA   Hardison L.K., Boczar B.A., Reynolds A.E., Cattolico R.A.;
RT   "A description of the Rubisco large subunit gene and its transcript in
RT   Olisthodiscus luteus.";
RL   Plant Mol. Biol. 18:595-599(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 470-488.
RC   STRAIN=Carter;
RX   PubMed=2740337; DOI=10.1073/pnas.86.13.4996;
RA   Boczar B.A., Delaney T.P., Cattolico R.A.;
RT   "Gene for the ribulose-1,5-bisphosphate carboxylase small subunit protein
RT   of the marine chromophyte Olisthodiscus luteus is similar to that of a
RT   chemoautotrophic bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:4996-4999(1989).
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       {ECO:0000255|HAMAP-Rule:MF_01338}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01338};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
CC   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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       {ECO:0000255|HAMAP-Rule:MF_01338}.
CC   -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR   EMBL; X61918; CAA43920.1; -; Genomic_DNA.
DR   EMBL; M24288; AAA84531.1; -; Genomic_DNA.
DR   PIR; S20506; S20506.
DR   AlphaFoldDB; P14959; -.
DR   SMR; P14959; -.
DR   PRIDE; P14959; -.
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: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   3: Inferred from homology;
KW   Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid.
FT   CHAIN           1..488
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062549"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   ACT_SITE        297
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /note="in homodimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         208
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   BINDING         382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   SITE            337
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT   MOD_RES         205
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
SQ   SEQUENCE   488 AA;  54000 MW;  38989C1742435534 CRC64;
     MSNNVYERNR IKNDRYESGV IPYAKMGYWD ANYSVKDTDL LALFRLTPQP GVDPVEAAAA
     VAGESSTATW TVVWTDLLTA CDVYRAKAYR VDPVPSAADQ YFAYIAYECD LFEEGSLANM
     TASIIGNVFG FKAVAALRLE DMRIPYAYLK TFQGPATGII VERERLDTFG RPLLGATVKP
     KLGLSGKNYG RVVYEGLRGG IDFLKDDENI NSQPFMRWRE RFLYCMEGIN RASAASGEVK
     GSYLNVTAAT MEEMYERADY AKAVGSVIVM IDLVIGYTAI QSMAIWARKN DMILHLHRAG
     NSTYARQKNH GINFRVICKW MRMAGVDHIH AGTVVGKLEG DPLMVKGFYD VLRETELSIN
     LPQGIFFEMD WASLRKCCPV ASGGIHCGQM HQLVYYLGDD VVLQFGGGTI GHPDGIQAGA
     TANRVALEAM ILARNEGRDY VSEGPEILRD IAKLCGPLKT ALDLWKGITF NYTSTDTADF
     VETATSNP
 
 
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