ID G5CCM0_9APIA Unreviewed; 247 AA. AC G5CCM0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 16-MAR-2016, entry version 18. 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:AEQ30017.1}; OS Angelica anomala. OG Plastid; Chloroplast {ECO:0000313|EMBL:AEQ30017.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Apiales; Apiaceae; Apioideae; OC apioid superclade; Selineae; Angelica. OX NCBI_TaxID=357845 {ECO:0000313|EMBL:AEQ30017.1}; RN [1] {ECO:0000313|EMBL:AEQ30017.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22397381; RA He Y., Hou P., Fan G., Song Z., Arain S., Shu H., Tang C., Yue Q., RA Zhang Y.; RT "Authentication of Angelica anomala Ave-Lall cultivars through DNA RT barcodes."; RL Mitochondrial DNA 23:100-105(2012). CC -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose CC 1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|RuleBase:RU000302}. CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = CC D-ribulose 1,5-bisphosphate + O(2). CC {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:RU000303}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. CC {ECO:0000256|RuleBase:RU004228}. 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; JN033544; AEQ30017.1; -; 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.110; -; 1. DR Gene3D; 3.30.70.150; -; 1. DR InterPro; IPR020878; RuBisCo_large_chain_AS. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 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:RU000303, KW ECO:0000313|EMBL:AEQ30017.1}; Lyase {ECO:0000256|RuleBase:RU000302}; KW Monooxygenase {ECO:0000256|RuleBase:RU000302}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|RuleBase:RU004237}; KW Plastid {ECO:0000313|EMBL:AEQ30017.1}. FT DOMAIN 24 144 RuBisCO_large_N. {ECO:0000259|Pfam: FT PF02788}. FT DOMAIN 154 246 RuBisCO_large. {ECO:0000259|Pfam: FT PF00016}. FT NON_TER 247 247 {ECO:0000313|EMBL:AEQ30017.1}. SQ SEQUENCE 247 AA; 27331 MW; E8EC4ADAE8CA2020 CRC64; MSPQTETKAG VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYGIEPV AGEENQFIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL NATAGTC //