RBL_PINPS
ID RBL_PINPS Reviewed; 48 AA.
AC P81080;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE Short=RuBisCO large subunit;
DE EC=4.1.1.39;
DE AltName: Full=Water stress-responsive protein 1/2/14;
DE Flags: Fragments;
GN Name=rbcL;
OS Pinus pinaster (Maritime pine).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=71647;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Needle;
RX PubMed=9747804; DOI=10.1023/a:1006006132120;
RA Costa P., Bahrman N., Frigerio J.-M., Kremer A., Plomion C.;
RT "Water-deficit-responsive proteins in maritime pine.";
RL Plant Mol. Biol. 38:587-596(1998).
RN [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Needle;
RX PubMed=10344291;
RX DOI=10.1002/(sici)1522-2683(19990101)20:4/5<1098::aid-elps1098>3.0.co;2-z;
RA Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A.,
RA Frigerio J.-M., Plomion C.;
RT "Separation and characterization of needle and xylem maritime pine
RT proteins.";
RL Electrophoresis 20:1098-1108(1999).
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 -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- INDUCTION: By water stress.
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 AlphaFoldDB; P81080; -.
DR SMR; P81080; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IPR036422; RuBisCO_lsu_N_sf.
DR SUPFAM; SSF54966; SSF54966; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Direct protein sequencing; Lyase; Monooxygenase; Oxidoreductase;
KW Photorespiration; Photosynthesis; Plastid; Stress response.
FT CHAIN <1..>48
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062563"
FT NON_CONS 24..25
FT /evidence="ECO:0000305"
FT NON_CONS 35..36
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 48
SQ SEQUENCE 48 AA; 5138 MW; DB2A46D34CC8F9D5 CRC64;
DTDILAAFRV TPQPGVPPEE AGAADVTLGF VDLLRWSPEL AAACEIWK
