ID A0A344X9G4_9LAMI Unreviewed; 416 AA. AC A0A344X9G4; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 11-DEC-2019, entry version 8. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|RuleBase:RU000302}; DE EC=4.1.1.39 {ECO:0000256|RuleBase:RU000302}; DE Flags: Fragment; GN Name=rbcL {ECO:0000313|EMBL:AXE75480.1}; OS Salvia cavaleriei var. cavaleriei. OG Plastid; Chloroplast {ECO:0000313|EMBL:AXE75480.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salvia; OC Salvia incertae sedis. OX NCBI_TaxID=1208401 {ECO:0000313|EMBL:AXE75480.1}; RN [1] {ECO:0000313|EMBL:AXE75480.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29945172; RA Hu G.X., Takano A., Drew B.T., Liu E.D., Soltis D.E., Soltis P.S., Peng H., RA Xiang C.L.; RT "Phylogeny and staminal evolution of Salvia (Lamiaceae, Nepetoideae) in RT East Asia."; RL Ann. Bot. 0:0-0(2018). RN [2] {ECO:0000313|EMBL:AXE75480.1} RP NUCLEOTIDE SEQUENCE. RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.; RL Submitted (JAN-2018) 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|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|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. CC {ECO:0000256|RuleBase:RU000302}. 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; MG823791; AXE75480.1; -; Genomic_DNA. DR EMBL; MG823792; AXE75481.1; -; Genomic_DNA. 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 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 Calvin cycle {ECO:0000256|RuleBase:RU000302}; KW Carbon dioxide fixation {ECO:0000256|RuleBase:RU000302}; KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:AXE75480.1}; KW Lyase {ECO:0000256|RuleBase:RU000302}; KW Magnesium {ECO:0000256|RuleBase:RU000302}; KW Metal-binding {ECO:0000256|RuleBase:RU000302}; KW Monooxygenase {ECO:0000256|RuleBase:RU000302}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000302}; KW Photorespiration {ECO:0000256|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|RuleBase:RU000302}; KW Plastid {ECO:0000313|EMBL:AXE75480.1}. FT DOMAIN 6..126 FT /note="RuBisCO_large_N" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 136..413 FT /note="RuBisCO_large" FT /evidence="ECO:0000259|Pfam:PF00016" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AXE75480.1" FT NON_TER 416 FT /evidence="ECO:0000313|EMBL:AXE75480.1" SQ SEQUENCE 416 AA; 46191 MW; BD036ABAA6E6D678 CRC64; EYKLTYYTPE YETKDTDILA AFRVTPQPGV PPEEAGAAVA AESSTGTWTT VWTDGLTSLD RYKGRCYHIE PVPGEKDQYI CYVAYPLDLF EEGSVTNMFT SIVGNVFGFK ALRALRLEDL RIPVAYVKTF QGPPHGIQVE RDKLNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS QPFMRWRDRF LFCAEAIYKA QTETGEIKGH YLNATAGTCE EMMKRAIFAR ELGVPIVMHD YLTGGFTANT TLAHYCRDNG LLLHIHRAMH AVIDRQKNHG MHFRVLAKAL RLSGGDHIHA GTVVGKLEGE RDITLGFVDL LRDDFVEKDR SRGIYFTQDW VSLPGVIPVA SGGIHVWHMP ALTEIFGDDS VLQFGGGTLG HPWGNAPGAV ANRVAVEACV QARNEG //