RBL_NANDO
ID RBL_NANDO Reviewed; 475 AA.
AC O20241; Q09FV3; Q40391;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 3.
DT 03-AUG-2022, entry version 109.
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: Precursor;
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338};
OS Nandina domestica (Heavenly bamboo).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Nandinoideae;
OC Nandina.
OX NCBI_TaxID=41776;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16934154; DOI=10.1186/1471-2229-6-17;
RA Moore M.J., Dhingra A., Soltis P.S., Shaw R., Farmerie W.G., Folta K.M.,
RA Soltis D.E.;
RT "Rapid and accurate pyrosequencing of angiosperm plastid genomes.";
RL BMC Plant Biol. 6:17-17(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-475.
RX AGRICOLA=IND20584463; DOI=10.2307/2419666;
RA Kim Y.-D., Jansen R.K.;
RT "Phylogenetic implications of rbcL and its sequence variation in the
RT Berberidaceae.";
RL Syst. Bot. 21:381-396(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-475.
RA Hoot S.B., Culham A., Crane P.R.;
RT "The utility of atpB gene sequences in resolving phylogenetic
RT relationships: comparison with rbcL and 18S ribosomal DNA sequences in the
RT Lardizabalaceae.";
RL Ann. Mo. Bot. Gard. 82:194-207(1995).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA70380.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ923117; ABI49871.1; -; Genomic_DNA.
DR EMBL; L75843; AAB63958.2; -; Genomic_DNA.
DR EMBL; L37920; AAA70380.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_740658.1; NC_008336.1.
DR AlphaFoldDB; O20241; -.
DR SMR; O20241; -.
DR GeneID; 4271604; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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 Acetylation; Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Disulfide bond; Lyase; Magnesium; Metal-binding; Methylation;
KW Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid.
FT PROPEP 1..2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT /id="PRO_0000262594"
FT CHAIN 3..475
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000062536"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 201
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 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 3
FT /note="N-acetylproline"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 14
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT CONFLICT 23
FT /note="N -> T (in Ref. 3; AAA70380)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="D -> E (in Ref. 3; AAA70380)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="T -> S (in Ref. 3; AAA70380)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="H -> P (in Ref. 3; AAA70380)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="A -> E (in Ref. 2 and 3; AAA70380/AAB63958)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="C -> S (in Ref. 2 and 3; AAA70380/AAB63958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 52677 MW; B7641626F6012CC9 CRC64;
MSPQTETKAS VGFKAGVKDY KLNYYTPDYV TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEDNQYICY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL RALRLEDLRI PTSYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEALFKAQA ETGEIKGHYL
NATAGTCEEM MKRAVFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV
IDRQKNHGIH FRVLAKALRM SGGDHIHAGT VVGKLEGERE ITLGFVDLLR DDFIEKDRSR
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVQA RNEGRDLARE GNEIIRAACK WSPELAAACE VWKEIKFEFE AMDTL
