ID A0A1B1YYY2_9POAL Unreviewed; 477 AA. AC A0A1B1YYY2; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 18-JAN-2017, entry version 3. 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:0000313|EMBL:ANX10396.1}; GN Synonyms=cbbL {ECO:0000256|HAMAP-Rule:MF_01338}; GN ORFNames=KudenCp030 {ECO:0000313|EMBL:ANX10396.1}; OS Kuruna densifolia. OG Plastid {ECO:0000313|EMBL:ANX10396.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Bambusoideae; Arundinarodae; Arundinarieae; Arundinariinae; Kuruna. OX NCBI_TaxID=1870832 {ECO:0000313|EMBL:ANX10396.1}; RN [1] {ECO:0000313|EMBL:ANX10396.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=27164472; DOI=10.1016/j.ympev.2016.05.008; RA Attigala L., Wysocki W.P., Duvall M.R., Clark L.G.; RT "Phylogenetic estimation and morphological evolution of Arundinarieae RT (Bambusoideae: Poaceae) based on plastome phylogenomic analysis."; RL Mol. Phylogenet. Evol. 101:111-121(2016). 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. Both reactions occur simultaneously and in competition CC at the same active site. {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 CC {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; KU569970; ANX10396.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-HAMAP. 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; 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 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|RuleBase:RU000302}; KW Photosynthesis {ECO:0000256|RuleBase:RU000302}; KW Plastid {ECO:0000313|EMBL:ANX10396.1}. 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 477 AA; 52790 MW; 357B38B224DBD1F1 CRC64; MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV VGEENQYIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPTYSKTFQG PPHGIQVERD KLNKYGRPFL GCTIKPKLGL SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKSQA ETGEIKGHYL NATAGTCEEM MKRAIFAREL GVPIVMPVSL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE MTLGFVDLLR DDFIEKDRAR GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVASEACVQA RNEGRDLAXX XXXXXXXXXX XSPELAAACE IWKAIKFEFE PVDKLDK //