RBL_CALSH
ID RBL_CALSH Reviewed; 459 AA.
AC P48687;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-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: Fragment;
GN Name=rbcL;
OS Calyptrosphaera sphaeroidea.
OG Plastid; Chloroplast.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Coccosphaerales;
OC Calyptrosphaeraceae; Calyptrosphaera.
OX NCBI_TaxID=35139;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fujiwara S., Sawada M., Someya J., Minaka N., Kawachi M., Inoue I.;
RT "Molecular phylogenetic analysis of rbcL in the Prymnesiophyta.";
RL J. Phycol. 30:863-871(1995).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
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; D45842; BAA08276.1; -; Genomic_DNA.
DR AlphaFoldDB; P48687; -.
DR SMR; P48687; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd08212; RuBisCO_large_I; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR InterPro; IPR020888; RuBisCO_lsuI.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 3: Inferred from homology;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium;
KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid.
FT CHAIN <1..459
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062393"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 308
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT NON_TER 1
SQ SEQUENCE 459 AA; 50552 MW; 37C230CD90BE077D CRC64;
DPEYAIKETD LLALFRCTPQ PGVDPVEAAA ALAGESSTAT WTVVWTDLLT ACDLYRAKAY
RVDPVPSAAD TYFCYIAYDI DLFEEGSLAN LTASIIGNIF GFKAVKALRL EDMRMPYALL
KTYQGPATGL VVERERLDKF GRPLLGATVK PKLGLSGKNY GRVVFEGLKG GLDFLKDDEN
INSQPFMRYR ERFLYSMEGV NHAAAMTGEV KGHYLNTTGA TMEDMYERAD FAKELGSVIV
MIDLVIGYTA IQSMAKWSRK TDMILHLHRA GNSTYSRQKT HGMNFRVICK WMRMSGVDHI
HAGTVVGKLE GDPLMIKGFY NTLLDFKTDV NLPQGLFFAQ DWASLRKCVP VASGGIHCGQ
MHQLINYLGD DVVLQFGGGT IGHPDGIQAG ATANRVALEA MVIARNEGRD YISEGPQILR
DAAKTCGPLQ TALDLWKDIT FNYASTDTAD FVETPTANV
