ID C8CJN9_PHAVU Unreviewed; 181 AA.
AC C8CJN9;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|RuleBase:RU000302};
DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|RuleBase:RU000302};
DE Flags: Fragment;
GN Name=rbcL {ECO:0000313|EMBL:ACV31768.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ACV31768.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ACV31768.1};
RN [1] {ECO:0000313|EMBL:ACV31768.1}
RP NUCLEOTIDE SEQUENCE.
RA Nicole S., Erickson D.L., Ambrosi D., Bellucci E., Lucchin M., Papa R.,
RA Kress W.J., Barcaccia G.;
RT "Biodiversity studies in Phaseolus spp. by DNA barcoding.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001067,
CC ECO:0000256|RuleBase:RU000302};
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:0000256|ARBA:ARBA00000537,
CC ECO:0000256|RuleBase:RU000302};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU000302};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU000302};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains.
CC {ECO:0000256|RuleBase:RU000302}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|RuleBase:RU000302}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000256|ARBA:ARBA00006204}.
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DR EMBL; GQ411617; ACV31768.1; -; Genomic_DNA.
DR EMBL; GQ411618; ACV31769.1; -; Genomic_DNA.
DR EMBL; GQ411619; ACV31770.1; -; Genomic_DNA.
DR EMBL; GQ411620; ACV31771.1; -; Genomic_DNA.
DR EMBL; GQ411621; ACV31772.1; -; Genomic_DNA.
DR EMBL; GQ411622; ACV31773.1; -; Genomic_DNA.
DR EMBL; GQ411623; ACV31774.1; -; Genomic_DNA.
DR EMBL; GQ411624; ACV31775.1; -; Genomic_DNA.
DR EMBL; GQ411625; ACV31776.1; -; Genomic_DNA.
DR EMBL; GQ411626; ACV31777.1; -; Genomic_DNA.
DR EMBL; GQ411627; ACV31778.1; -; Genomic_DNA.
DR EMBL; GQ411628; ACV31779.1; -; Genomic_DNA.
DR EMBL; GQ411629; ACV31780.1; -; Genomic_DNA.
DR EMBL; GQ411630; ACV31781.1; -; Genomic_DNA.
DR EMBL; GQ411631; ACV31782.1; -; Genomic_DNA.
DR EMBL; GQ411632; ACV31783.1; -; Genomic_DNA.
DR EMBL; GQ411633; ACV31784.1; -; Genomic_DNA.
DR EMBL; GQ411634; ACV31785.1; -; Genomic_DNA.
DR EMBL; GQ411635; ACV31786.1; -; Genomic_DNA.
DR EMBL; GQ411636; ACV31787.1; -; Genomic_DNA.
DR EMBL; GQ411637; ACV31788.1; -; Genomic_DNA.
DR EMBL; GQ411638; ACV31789.1; -; Genomic_DNA.
DR EMBL; GQ411639; ACV31790.1; -; Genomic_DNA.
DR EMBL; GQ411640; ACV31791.1; -; Genomic_DNA.
DR EMBL; GQ411641; ACV31792.1; -; Genomic_DNA.
DR EMBL; GQ411642; ACV31793.1; -; Genomic_DNA.
DR EMBL; GQ411643; ACV31794.1; -; Genomic_DNA.
DR EMBL; GQ411644; ACV31795.1; -; Genomic_DNA.
DR EMBL; GQ411645; ACV31796.1; -; Genomic_DNA.
DR EMBL; GQ411646; ACV31797.1; -; Genomic_DNA.
DR EMBL; GQ411647; ACV31798.1; -; Genomic_DNA.
DR EMBL; GQ411648; ACV31799.1; -; Genomic_DNA.
DR EMBL; GQ411649; ACV31800.1; -; Genomic_DNA.
DR EMBL; GQ411650; ACV31801.1; -; Genomic_DNA.
DR EMBL; GQ411651; ACV31802.1; -; Genomic_DNA.
DR EMBL; GQ411652; ACV31803.1; -; Genomic_DNA.
DR EMBL; GQ411653; ACV31804.1; -; Genomic_DNA.
DR AlphaFoldDB; C8CJN9; -.
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; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 3: Inferred from homology;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567,
KW ECO:0000256|RuleBase:RU000302};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300,
KW ECO:0000256|RuleBase:RU000302};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|RuleBase:RU000302};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000302};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000302};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000302};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000302};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000302};
KW Photorespiration {ECO:0000256|ARBA:ARBA00023238,
KW ECO:0000256|RuleBase:RU000302};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ACV31768.1}.
FT DOMAIN 1..107
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 117..181
FT /note="Ribulose bisphosphate carboxylase large subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00016"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV31768.1"
FT NON_TER 181
FT /evidence="ECO:0000313|EMBL:ACV31768.1"
SQ SEQUENCE 181 AA; 20213 MW; 08FC2643B2DF934E CRC64;
AAFRVTPQPG VPPEEAGAAV AAESSTGTWT TVWTDGLTSL DRYKGRCYHI EPVAGEENQF
IAYVAYPLDL FEEGSVTNMF TSIVGNVFGF KALRALRLED LRIPTAYIKT FQGPPHGIQV
ERDKLNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN SQPFMRWRDR
F
//