ID G8D4P9_EQUVA Unreviewed; 184 AA.
AC G8D4P9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:ADR72379.1};
OS Equisetum variegatum (Variegated horsetail).
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADR72379.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Equisetidae; Equisetales; Equisetaceae; Equisetum.
OX NCBI_TaxID=231678 {ECO:0000313|EMBL:ADR72379.1};
RN [1] {ECO:0000313|EMBL:ADR72379.1}
RP NUCLEOTIDE SEQUENCE.
RA Burgess K.S., Fazekas A.J., Kesanakurti P.R., Graham S.W., Husband B.C.,
RA Newmaster S.G., Percy D.M., Hajibabaei M., Barrett S.C.H.;
RT "Discriminating plant species in a local temperate flora using the
RT rbcL+matK DNA barcode.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV44046.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23190419; DOI=10.1186/1472-6785-12-25;
RA Kuzmina M.L., Johnson K.L., Barron H.R., Hebert P.D.;
RT "Identification of the vascular plants of Churchill, Manitoba, using a DNA
RT barcode library.";
RL BMC Ecol. 12:25-25(2012).
RN [3] {ECO:0000313|EMBL:AGH04416.1}
RP NUCLEOTIDE SEQUENCE.
RA Saarela J.M., Sokoloff P.C., Gillespie L.J., Consaul L.L., Bull R.D.;
RT "DNA Barcoding the Canadian Arctic Flora: Core Plastid Barcodes (rbcL +
RT matK) for 490 Vascular Plant Species.";
RL PLoS ONE 8:E77982-E77982(2013).
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:0000256|ARBA:ARBA00025664}.
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 disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers. {ECO:0000256|ARBA:ARBA00025888}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {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; HQ590086; ADR72379.1; -; Genomic_DNA.
DR EMBL; JN965527; AEV44046.1; -; Genomic_DNA.
DR EMBL; KC482741; AGH04416.1; -; Genomic_DNA.
DR EMBL; KC482743; AGH04418.1; -; Genomic_DNA.
DR EMBL; KC482745; AGH04420.1; -; Genomic_DNA.
DR EMBL; KC482746; AGH04421.1; -; Genomic_DNA.
DR EMBL; KC482748; AGH04423.1; -; Genomic_DNA.
DR EMBL; KC482749; AGH04424.1; -; Genomic_DNA.
DR EMBL; KC482750; AGH04425.1; -; Genomic_DNA.
DR EMBL; KC482752; AGH04427.1; -; Genomic_DNA.
DR EMBL; KC482753; AGH04428.1; -; Genomic_DNA.
DR EMBL; KC482754; AGH04429.1; -; Genomic_DNA.
DR EMBL; KC482755; AGH04430.1; -; Genomic_DNA.
DR EMBL; KC482756; AGH04431.1; -; Genomic_DNA.
DR EMBL; KC482759; AGH04434.1; -; Genomic_DNA.
DR EMBL; KC482760; AGH04435.1; -; Genomic_DNA.
DR AlphaFoldDB; G8D4P9; -.
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; 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.
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|RuleBase:RU000302, ECO:0000313|EMBL:ADR72379.1};
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 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|RuleBase:RU000302};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ADR72379.1}.
FT DOMAIN 15..135
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 145..184
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:ADR72379.1"
FT NON_TER 184
FT /evidence="ECO:0000313|EMBL:ADR72379.1"
SQ SEQUENCE 184 AA; 20285 MW; A973B5281861AE27 CRC64;
GVGFKAGVKD YRLTYFTPDY ETKETDILAA FRMTPQPGVP PEEAGAAVAA ESSTGTWTTV
WTDGLTSLDR YKGRCYNIEP VAGEDNQFIA YVAYPLDLFE EGSVTNLFTS IVGNVFGFKA
LRALRLEDLR IPPAYSKTFI GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV
YECL
//
