ID G9DQ18_9ASTR Unreviewed; 199 AA.
AC G9DQ18;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 22-FEB-2023, entry version 31.
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:AEM05452.1};
OS Soroseris erysimoides.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEM05452.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Crepidinae; Soroseris.
OX NCBI_TaxID=996404 {ECO:0000313|EMBL:AEM05452.1};
RN [1] {ECO:0000313|EMBL:AEM05452.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22100737; DOI=10.1073/pnas.1104551108;
RG China Plant BOL Group;
RA Li D.Z., Gao L.M., Li H.T., Wang H., Ge X.J., Liu J.Q., Chen Z.D.,
RA Zhou S.L., Chen S.L., Yang J.B., Fu C.X., Zeng C.X., Yan H.F., Zhu Y.J.,
RA Sun Y.S., Chen S.Y., Zhao L., Wang K., Yang T., Duan G.W.;
RT "Comparative analysis of a large dataset indicates that internal
RT transcribed spacer (ITS) should be incorporated into the core barcode for
RT seed plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19641-19646(2011).
RN [2] {ECO:0000313|EMBL:AEM05452.1}
RP NUCLEOTIDE SEQUENCE.
RA Li D.-Z., Gao L.-M., Li H.-T., Wang H., Ge X.-J.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QKO00877.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu Y., Zeng C.-X., Zhang Y.-Q., Ren Y., Ge X.-J.;
RT "DNA barcoding the Flora of Qinling Mts. in China.";
RL Submitted (JUL-2019) 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 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; JF944478; AEM05452.1; -; Genomic_DNA.
DR EMBL; MN204770; QKO00877.1; -; Genomic_DNA.
DR AlphaFoldDB; G9DQ18; -.
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|RuleBase:RU000302, ECO:0000313|EMBL:AEM05452.1};
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:AEM05452.1}.
FT DOMAIN 3..123
FT /note="Ribulose bisphosphate carboxylase large subunit
FT ferrodoxin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02788"
FT DOMAIN 133..198
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:AEM05452.1"
FT NON_TER 199
FT /evidence="ECO:0000313|EMBL:AEM05452.1"
SQ SEQUENCE 199 AA; 22311 MW; 9DF8E7EC4CB22508 CRC64;
LTYYTPDYET KDTDILAAFR VTPQPGVPPE EAGAAVAAES STGTWTTVWT DGLTSLDRYK
GRCYGIEPVP GEESQFIAYV AYPLDLFEEG SVTNMFTSIV GNVFGFKALR ALRLEDLRIP
TAYVKTFQGP PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE CLRGGLDFTK
DDENVNSQPF MRWRDRFLF
//
