RBL_ADIPE
ID RBL_ADIPE Reviewed; 413 AA.
AC P43223;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Adiantum pedatum (Northern maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=29590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=8202555; DOI=10.1073/pnas.91.12.5730;
RA Hasebe M., Omori T., Nakazawa M., Sano T., Kato M., Iwatsuki K.;
RT "rbcL gene sequences provide evidence for the evolutionary lineages of
RT leptosporangiate ferns.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5730-5734(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 -!- 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 disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000250}.
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; U05602; AAA19886.1; -; Genomic_DNA.
DR AlphaFoldDB; P43223; -.
DR SMR; P43223; -.
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; Disulfide bond; Lyase;
KW Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration;
KW Photosynthesis; Plastid.
FT CHAIN <1..>413
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062341"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 311
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 178
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT DISULFID 224
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 413
SQ SEQUENCE 413 AA; 45751 MW; C3DE2ED825DFFC04 CRC64;
YYTPEYKTKD TDILAAFRMT PQPGVPAEEA GAAVAAESST GTWTTVWTDG LTSLDRYKGR
CYDIEPVAGE ENQYIAYVAY PLDLFEEGSV TNMLTSIVGN VFGFKALRAL RLEDLRIPPA
YSKTFMGPPH GIQVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD
ENVNSQPFMR WRDRFLFVAE ALFKSQAETG EIKGHYLNAT AGTCEEMMKR AVFARELGAP
IVMHDYLTGG FTANTSLAFY CRDNGLLLHI HRAMHAVIDR QRNHGIHFRV LAKALRMSGG
DHIHAGTVVG KLEGEREVTL GFVDLLRDDY IEKDRSRGIY FTQDWVSMPG VFPVASGGIH
VWHMPALTEI FGDDSVLQFG GGTLGHPWGN APGAVANRVA LEACVQARNE GRD
