RBL_VITSX
ID RBL_VITSX Reviewed; 55 AA.
AC P85085;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39;
DE Flags: Fragments;
GN Name=rbcL {ECO:0000250|UniProtKB:P00876};
OS Vitis sp. (Grape).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis; unclassified Vitis.
OX NCBI_TaxID=3604;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND INDUCTION.
RC STRAIN=V.simpsonii cv. Pixiola X V.vinifera cv. Golden Muscat
RC {ECO:0000269|PubMed:18931950}; TISSUE=Leaf {ECO:0000269|PubMed:18931950};
RX PubMed=18931950; DOI=10.1007/s12010-008-8380-3;
RA Vasanthaiah H.K.N., Katam R., Basha S.M.;
RT "Characterization of unique and differentially expressed proteins in
RT anthracnose-tolerant Florida hybrid bunch grapes.";
RL Appl. Biochem. Biotechnol. 157:395-406(2009).
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|UniProtKB:P00876}.
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 Evidence={ECO:0000250|UniProtKB:P00876};
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:0000250|UniProtKB:P00876};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00876};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00876};
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|UniProtKB:P00876}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: By E.ampelina infection. {ECO:0000269|PubMed:18931950}.
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|UniProtKB:P00876}.
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|UniProtKB:P00876}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255}.
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DR PRIDE; P85085; -.
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 InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR SUPFAM; SSF51649; SSF51649; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Direct protein sequencing; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid.
FT CHAIN <1..>55
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000280227"
FT ACT_SITE 18
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00876"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00876"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00876"
FT SITE 34
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00876"
FT NON_CONS 11..12
FT /evidence="ECO:0000303|PubMed:18931950"
FT NON_CONS 19..20
FT /evidence="ECO:0000303|PubMed:18931950"
FT NON_CONS 34..35
FT /evidence="ECO:0000303|PubMed:18931950"
FT NON_CONS 45..46
FT /evidence="ECO:0000303|PubMed:18931950"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:18931950"
FT NON_TER 55
FT /evidence="ECO:0000303|PubMed:18931950"
SQ SEQUENCE 55 AA; 6102 MW; 421AC534607A4D47 CRC64;
LTYYTPEYET KGLLLHXHRM SGGDHIHAGX VVGKEITLGF VDLLRVALEA CVQAR
