RBL_ILECI
ID RBL_ILECI Reviewed; 54 AA.
AC P31192;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 92.
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 ciliospinosa (Sichuan 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=4299;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; X69742; CAA49397.1; -; Genomic_DNA.
DR PIR; S31528; S31528.
DR AlphaFoldDB; P31192; -.
DR SMR; P31192; -.
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_0000031261"
FT CHAIN 3..>54
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000031262"
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; 5880 MW; FFEACF5AE81103F8 CRC64;
MSPQTETKAS VGFKAGVKDY KLNYYTPDYV TKDTDILAAF RVSPQPGVPP EEAG
