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RBL_PORCA
ID   RBL_PORCA               Reviewed;         488 AA.
AC   P50255; Q760S5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 102.
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   Pyropia suborbiculata (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Pyropia.
OX   NCBI_TaxID=1185355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Thallus;
RA   Kito H., Kunimoto M., Mizukami Y., Murase N., Kuroki T., Taruta M.,
RA   Levine I.;
RT   "Species determination utilizing Porphyra (Rhodophyta) plastid DNA RuBisCo
RT   sequences.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-488.
RX   PubMed=8041781; DOI=10.1073/pnas.91.15.7281;
RA   Freshwater D.W., Fredericq S., Butler B.S., Hommersand M.H., Chase M.W.;
RT   "A gene phylogeny of the red algae (Rhodophyta) based on plastid rbcL.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7281-7285(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.
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; AB118580; BAC84927.1; -; Genomic_DNA.
DR   EMBL; U04041; AAB16952.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50255; -.
DR   SMR; P50255; -.
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_0000062573"
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"
FT   CONFLICT        88
FT                   /note="A -> R (in Ref. 2; AAB16952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116..117
FT                   /note="SI -> LY (in Ref. 2; AAB16952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="S -> A (in Ref. 2; AAB16952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        399
FT                   /note="D -> V (in Ref. 2; AAB16952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        424
FT                   /note="K -> R (in Ref. 2; AAB16952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="G -> E (in Ref. 2; AAB16952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="K -> E (in Ref. 2; AAB16952)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   488 AA;  54045 MW;  7C034C5C86DAE8DA CRC64;
     MSQSVESRTR IKSERYESGV IPYAKMGYWD ADYVIKETDI LALFRITPQP GVDPIEASAA
     IAGESSTATW TVVWTDLLTA CDLYRAKAYR VDPVPNVADQ YFAYIAYDID LFEEGSIANL
     TASIIGNVFG FKAVKALRLE DMRMPVAYLK TFQGPATGLI VERERMDKFG RPFLGATVKP
     KLGLSGKNYG RVVYEGLKGG LDFLKDDENI NSQPFMRWRE RFLYSMEGVN KASASAGEIK
     GHYLNVTAAT MEDMYERAEF SKEVGSIICM IDLVIGYTAI QSMAIWARKH DMILHLHRAG
     NSTYSRQKNH GMNFRVICKW MRMAGVDHIH AGTVVGKLEG DPLMIKGFYN TLLESETDIN
     LPQGLFFAQN WASLRKVVPV ASGGIHAGQM HQLLDYLGDD VVLQFGGGTI GHPDGIQAGA
     TANKVALESM VMARNEGRNY VAKGPQILRD AAKTCGPLQT ALDLWKDISF NYTSTDTADF
     VETPTANI
 
 
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