ID   RBL_ILEAQ               Reviewed;          54 AA.
AC   P31191;
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   Ilex aquifolium (English holly).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Aquifoliales; Aquifoliaceae; Ilex.
OX   NCBI_TaxID=4298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sample IAQ4;
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; X69741; CAA49396.1; -; Genomic_DNA.
DR   PIR; S31527; S31527.
DR   AlphaFoldDB; P31191; -.
DR   SMR; P31191; -.
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_0000031259"
FT   CHAIN           3..>54
FT                   /note="Ribulose bisphosphate carboxylase large chain"
FT                   /id="PRO_0000031260"
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         54
SQ   SEQUENCE   54 AA;  5867 MW;  10A12F5AE81103E3 CRC64;
     MSPQTETKAS VGFKAGVKDY KLTYYTPDYV TKDTDILAAF RVSPQPGVPP EEAG