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RBL_SOLLC
ID   RBL_SOLLC               Reviewed;         477 AA.
AC   P27065; Q2A7G1; Q2MI92;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 4.
DT   03-AUG-2022, entry version 134.
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   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND93053816; DOI=10.2307/2399855;
RA   Olmstead R.G., Bremer B., Scott K.M., Palmer J.D.;
RT   "A parsimony analysis of the Asteridae sensu lato based on rbcL
RT   sequences.";
RL   Ann. Mo. Bot. Gard. 80:700-722(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. LA3023;
RX   PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA   Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA   Tomkins J., Jansen R.K.;
RT   "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT   lycopersicum and comparative analyses with other Solanaceae genomes.";
RL   Theor. Appl. Genet. 112:1503-1518(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. IPA-6;
RX   PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA   Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT   "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT   solanaceous plastid genomes.";
RL   J. Mol. Evol. 63:194-207(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 3-18, METHYLATION AT LYS-14, AND ACETYLATION AT PRO-3.
RX   PubMed=16668742; DOI=10.1104/pp.98.3.1170;
RA   Houtz R.L., Poneleit L., Jones S.B., Royer M., Stults J.T.;
RT   "Posttranslational modifications in the amino-terminal region of the large
RT   subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from several
RT   plant species.";
RL   Plant Physiol. 98:1170-1174(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. 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; 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; L14403; AAA19771.1; -; Unassigned_DNA.
DR   EMBL; DQ347959; ABC56308.1; -; Genomic_DNA.
DR   EMBL; AM087200; CAJ32401.1; -; Genomic_DNA.
DR   PIR; PQ0795; PQ0795.
DR   RefSeq; AP_004936.1; AC_000188.1.
DR   RefSeq; YP_008563096.1; NC_007898.3.
DR   AlphaFoldDB; P27065; -.
DR   SMR; P27065; -.
DR   STRING; 4081.Solyc01g007330.2.1; -.
DR   iPTMnet; P27065; -.
DR   PaxDb; P27065; -.
DR   PRIDE; P27065; -.
DR   GeneID; 3950460; -.
DR   KEGG; sly:3950460; -.
DR   eggNOG; ENOG502QTI9; Eukaryota.
DR   HOGENOM; CLU_031450_2_0_1; -.
DR   InParanoid; P27065; -.
DR   OrthoDB; 474428at2759; -.
DR   PhylomeDB; P27065; -.
DR   Proteomes; UP000004994; Chloroplast.
DR   ExpressionAtlas; P27065; baseline.
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   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Direct protein sequencing; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW   Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid; Reference proteome.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT                   /id="PRO_0000031285"
FT   CHAIN           3..477
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000031286"
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            334
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         3
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT   MOD_RES         14
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT   MOD_RES         201
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        247
FT                   /note="Interchain; in linked form"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  52954 MW;  66CC07677A65C2B6 CRC64;
     MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
     SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY VAYPLDLFEE GSVTNMFTSI
     VGNVFGFKAL RALRLEDLRI PPAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
     SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQT ETGEIKGHYL
     NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
     IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFVEQDRSR
     GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
     RVALEACVKA RNEGRDLARE GNEIIREACK WSPELAAACE VWKEIVFNFA AVDVLDK
 
 
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