RBL_DROBR
ID RBL_DROBR Reviewed; 435 AA.
AC P28404;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Drosera burmannii (Burmese sundew).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Droseraceae; Drosera.
OX NCBI_TaxID=4365;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1523408; DOI=10.1126/science.1523408;
RA Albert V.A., Williams S.E., Chase M.W.;
RT "Carnivorous plants: phylogeny and structural evolution.";
RL Science 257:1491-1495(1992).
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.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01338};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
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. {ECO:0000255|HAMAP-Rule:MF_01338}.
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:0000255|HAMAP-Rule:MF_01338}.
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'.
CC {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; L01908; AAA16233.2; -; Genomic_DNA.
DR AlphaFoldDB; P28404; -.
DR SMR; P28404; -.
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 CDD; cd08212; RuBisCO_large_I; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01338; RuBisCO_L_type1; 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; Disulfide bond; Lyase;
KW Magnesium; Metal-binding; Methylation; Monooxygenase; Oxidoreductase;
KW Photorespiration; Photosynthesis; Plastid.
FT CHAIN <1..>435
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062447"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 114
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 325
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 192
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT DISULFID 238
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT NON_TER 1
FT NON_TER 435
SQ SEQUENCE 435 AA; 47990 MW; DB0FF6EBE840D85F CRC64;
SVGFKAGVKD YKLTYYTPDY QTLDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV
WTDGLTSLDR YKGRCYHIEP VAGEDNQYIV YVAYPLDLFE EGSVTNMFTS IVGNVFGFKA
LRALRLEDLR IPPAYSKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV
YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEAIFKAQ AETGEIKGHY LNATAGTCEE
MIKRAVFARE LGVPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGI
HFRVLAKALR LSGGDHIHSG TVVGKLEGER DITLGFVDLL RDDVIEKDRS RGIYFSQFWV
SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNPPGAAA NRVALEACVQ
ARNEGQDLAR EGNEI
