RBL_NUPVA
ID RBL_NUPVA Reviewed; 394 AA.
AC Q05801;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Nuphar variegata (Yellow pond lily) (Nuphar lutea subsp. variegata).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nuphar.
OX NCBI_TaxID=4416;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1946432; DOI=10.1073/pnas.88.22.10119;
RA Les D.H., Garvin D.K., Wimpee C.F.;
RT "Molecular evolutionary history of ancient aquatic angiosperms.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10119-10123(1991).
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; M77029; AAA84527.1; -; Genomic_DNA.
DR AlphaFoldDB; Q05801; -.
DR SMR; Q05801; -.
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:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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 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; Methylation; Monooxygenase; Oxidoreductase;
KW Photorespiration; Photosynthesis; Plastid.
FT CHAIN <1..>394
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062544"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 325
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT NON_TER 1
FT NON_TER 394
SQ SEQUENCE 394 AA; 43816 MW; E400510AD898C803 CRC64;
SVGFKAGVKD YRLTYYTPDY ETLATDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV
WTDGLTSLDR YKGRCYHIEP VPGEENQYIA YVAYPLDLFE EGSVTNMFTS IVGNVFGFKA
LRALRLEDLR IPPAYSKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV
YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEALYKAQ AETGEIKGHY LNATAGTSEE
MLKRAACARE LGVPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQRNHGI
HFRVLAKALR MSGGDHIHSG TVVGKLEGER DVTLGFVDLL RDDFIEKDRS RGIYFTQDWV
SMPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFG
