ID   RBL_VIGUU               Reviewed;          16 AA.
AC   P27067;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
DE   Flags: Fragment;
GN   Name=rbcL;
OS   Vigna unguiculata subsp. unguiculata (Cowpea) (Vigna sinensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3920;
RN   [1]
RP   PROTEIN SEQUENCE, METHYLATION AT LYS-12, AND ACETYLATION AT PRO-1.
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   -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC       {ECO:0000250}.
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' (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; P27067; -.
DR   iPTMnet; P27067; -.
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.
PE   1: Evidence at protein level;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW   Direct protein sequencing; Lyase; Methylation; Monooxygenase;
KW   Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
FT   CHAIN           1..>16
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000062611"
FT   MOD_RES         1
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT   MOD_RES         12
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000269|PubMed:16668742"
FT   NON_TER         16
SQ   SEQUENCE   16 AA;  1648 MW;  D0AD959A82688872 CRC64;
     PQTETKASVG FKAGVK