ID   RBL_WEISI               Reviewed;          58 AA.
AC   P31203;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Ribulose bisphosphate carboxylase large chain;
DE            Short=RuBisCO large subunit;
DE            EC=4.1.1.39;
DE   Flags: Precursor; Fragment;
GN   Name=rbcL;
OS   Weinmannia silvicola (Towai).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Oxalidales; Cunoniaceae; Weinmannia.
OX   NCBI_TaxID=3780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sample WSY2;
RX   PubMed=8025727; DOI=10.1006/mpev.1994.1004;
RA   Savolainen V., Manen J.F., Douzery E.J.P., Spichiger R.;
RT   "Molecular phylogeny of families related to Celastrales based on rbcL 5'
RT   flanking sequences.";
RL   Mol. Phylogenet. Evol. 3:27-37(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 (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   -!- 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; X69756; CAA49411.1; -; Genomic_DNA.
DR   PIR; S31541; S31541.
DR   AlphaFoldDB; P31203; -.
DR   SMR; P31203; -.
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   Gene3D; 3.30.70.150; -; 1.
DR   InterPro; IPR033966; RuBisCO.
DR   InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR   InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR   PANTHER; PTHR42704; PTHR42704; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SUPFAM; SSF54966; SSF54966; 1.
PE   3: Inferred from homology;
KW   Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase;
KW   Methylation; Monooxygenase; Oxidoreductase; Photorespiration;
KW   Photosynthesis; Plastid.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000031445"
FT   CHAIN           3..>58
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000031446"
FT   MOD_RES         3
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         14
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         58
SQ   SEQUENCE   58 AA;  6209 MW;  E2587F8D62900C5A CRC64;
     MSPQTETKAS VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVSPQPGVPP EEAGAAVA