ID A0A1Y0B577_9APIA Unreviewed; 475 AA. AC A0A1Y0B577; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 27-SEP-2017, entry version 2. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338}; DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01338, GN ECO:0000313|EMBL:ART32566.1}; OS Hansenia forbesii. OG Plastid; Chloroplast {ECO:0000313|EMBL:ART32566.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Apiales; Apiaceae; Apioideae; OC Physospermopsis clade; Hansenia. OX NCBI_TaxID=165499 {ECO:0000313|EMBL:ART32566.1}; RN [1] {ECO:0000313|EMBL:ART32566.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28422071; RA Yang J., Yue M., Niu C., Ma X.F., Li Z.H.; RT "Comparative Analysis of the Complete Chloroplast Genome of Four RT Endangered Herbals of Notopterygium."; RL Genes (Basel) 8:124-124(2017). 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|HAMAP-Rule:MF_01338}. CC -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose CC 1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}. CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = CC D-ribulose 1,5-bisphosphate + O(2). {ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}. CC -!- PTM: The disulfide bond which can form in the large chain dimeric CC partners within the hexadecamer appears to be associated with CC oxidative stress and protein turnover. {ECO:0000256|HAMAP- CC Rule:MF_01338}. CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large CC chain homodimer in a "head-to-tail" conformation. In form I CC RuBisCO this homodimer is arranged in a barrel-like tetramer with CC the small subunits forming a tetrameric "cap" on each end of the CC "barrel". {ECO:0000256|HAMAP-Rule:MF_01338}. 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; KX808492; ART32566.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; 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; IPR017443; RuBisCO_lsu_fd_N. DR InterPro; IPR020888; RuBisCO_lsuI. 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|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Chloroplast {ECO:0000256|RuleBase:RU000302, KW ECO:0000313|EMBL:ART32566.1}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01338}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Methylation {ECO:0000256|HAMAP-Rule:MF_01338}; KW Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Photorespiration {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Plastid {ECO:0000313|EMBL:ART32566.1}. FT DOMAIN 24 144 RuBisCO_large_N. {ECO:0000259|Pfam: FT PF02788}. FT DOMAIN 154 462 RuBisCO_large. {ECO:0000259|Pfam: FT PF00016}. FT ACT_SITE 175 175 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT ACT_SITE 294 294 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT METAL 201 201 Magnesium; via carbamate group. FT {ECO:0000256|HAMAP-Rule:MF_01338}. FT METAL 203 203 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT METAL 204 204 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 123 123 Substrate; in homodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01338}. FT BINDING 173 173 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 177 177 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 295 295 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 327 327 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 379 379 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT SITE 334 334 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01338}. FT MOD_RES 14 14 N6,N6,N6-trimethyllysine. FT {ECO:0000256|HAMAP-Rule:MF_01338}. FT MOD_RES 201 201 N6-carboxylysine. {ECO:0000256|HAMAP- FT Rule:MF_01338}. FT DISULFID 247 247 Interchain; in linked form. FT {ECO:0000256|HAMAP-Rule:MF_01338}. SQ SEQUENCE 475 AA; 52552 MW; 8C78C3FDFA0AF0F3 CRC64; MSPQTETKAG VGFKAGVKDY KLTYYTPDYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYGIEPV AGEENQYIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PVAYVKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM MKRAIFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR DDFIEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLASE GNEIIREATK WSPELAAACE VWKEIKFEFQ AMDTL //