ID A0A3G1N1M1_ABIGR Unreviewed; 184 AA. AC A0A3G1N1M1; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 22-FEB-2023, entry version 17. 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:AUR44199.1}; OS Abies grandis (Grand fir) (Pinus grandis). OG Plastid; Chloroplast {ECO:0000313|EMBL:AUR44199.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies. OX NCBI_TaxID=46611 {ECO:0000313|EMBL:AUR44199.1}; RN [1] {ECO:0000313|EMBL:AUR44199.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29299394; DOI=10.3732/apps.1700079; RA Kuzmina M.L., Braukmann T.W.A., Fazekas A.J., Graham S.W., Dewaard S.L., RA Rodrigues A., Bennett B.A., Dickinson T.A., Saarela J.M., Catling P.M., RA Newmaster S.G., Percy D.M., Fenneman E., Lauron-Moreau A., Ford B., RA Gillespie L., Subramanyam R., Whitton J., Jennings L., Metsger D., RA Warne C.P., Brown A., Sears E., Dewaard J.R., Zakharov E.V., Hebert P.D.N.; RT "Using herbarium-derived DNAs to assemble a large-scale DNA barcode library RT for the vascular plants of Canada."; RL Appl Plant Sci 5:0-0(2017). 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|RuleBase:RU000302}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {ECO:0000256|ARBA:ARBA00006204}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MG215142; AUR44199.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3G1N1M1; -. 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:AUR44199.1}; 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:AUR44199.1}. 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:AUR44199.1" FT NON_TER 184 FT /evidence="ECO:0000313|EMBL:AUR44199.1" SQ SEQUENCE 184 AA; 20327 MW; 00A85FD0998BCA35 CRC64; SVGFKAGVKD YRLTYYTPEY QTKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV WTDGLTSLDR YKGRCYDIEP VPGEESQFIA YVAYPLDLFE EGSVTNLFTS IVGNVFGFKA LRALRLEDLR IPPAYSKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECL //