RBL_ARTBA
ID RBL_ARTBA Reviewed; 416 AA.
AC P43225;
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 Arthropteris beckleri (Fern) (Polypodium beckleri).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Polypodiineae; Tectariaceae;
OC Arthropteris.
OX NCBI_TaxID=29631;
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; U05605; AAA19889.1; -; Genomic_DNA.
DR AlphaFoldDB; P43225; -.
DR SMR; P43225; -.
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..>416
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062362"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
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 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 180
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10114"
FT DISULFID 226
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 416
SQ SEQUENCE 416 AA; 45945 MW; 46BB08E5B29D68CF CRC64;
LTYYTPDYQT KDTDILAAFR MTPQPGVPAE EAGAAVAAES STGTWTTVWT DGLTSLDRYK
GRCYDIEPVA GEENQYIAYV AYPLDLFEEG SVTNLFTSIV GNVFGFKALR ALRLEDLRIP
PAYSKTFIGP PHGIQVERDK LTKYGRPLLG CTIKPKLGLS AKNYGRAVYE CLRGGLDFTK
DDENVNSQPF MRWRDRFLSV AEALFKAQAE TGEIKGHYLN ATAGTCEEMM KRAIFARELG
APIVMHDYLT GGFTANTSLA YYCRDNGLLL HIHRAMHAVI DRQRNHGMHF RVLAKALRMS
GGDHVHAGTV VGKLEGERDV TLGFVDLLRD DYIEKDRSRG VYFTQDWVSM PGVIPVASGG
IHVWHMPALT EIFGDDSVLQ FGGGTLGHPW GNAPGAVANR VALEACVQAR NEGRDL
