RBL_VANST
ID RBL_VANST Reviewed; 406 AA.
AC P43229;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, 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 Vandenboschia striata (Fern) (Crepidomanes birmanicum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Hymenophyllales; Hymenophyllaceae;
OC Trichomanoideae; Vandenboschia.
OX NCBI_TaxID=29625;
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; U05613; AAA19897.1; -; Genomic_DNA.
DR AlphaFoldDB; P43229; -.
DR SMR; P43229; -.
DR PRIDE; P43229; -.
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..>406
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062427"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
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 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 312
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT DISULFID 225
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 406
SQ SEQUENCE 406 AA; 44888 MW; 47137F9AED3F7950 CRC64;
NYYTPDYETK GTDILAAFRM TPQPGVPPEE AGAAVAAESS TGTWTTVWTD GLTSLDRYKG
RCYDIEPVAG EEHQFIAYVA YPLDLFEEGS VTNLFTSIVG NVFGFKALRA LRLGDLRIPP
SYSKTFMGPP HGIQVERDKL NKYGRPFLGC TIKPKLGLSA KNYGRAVYEC LRGGLDFTKD
DENVNSQPFM RWRDRFLFVA EALFKAQSET GEVKGHYLNA TAGTCEEMFK RAIFARELGA
PIVMHDYLTG GFTANTSLAY YCRDNGLLLH IHRAMHAVID RQKNHGMHFR VLAKALRMSG
GDHFHSGTVV GKLEGERDIT LGFVDLLRDD YIDKDRSRGI YFTQDWVSMP GVLPVASGGI
HVWHMPALTE IFGDDSVLQF GGGTLGHPWG NAPGAVANRV ALVACV
