ID H2F581_ASPOF Unreviewed; 480 AA. AC H2F581; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 12-APR-2017, entry version 30. 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:AEX93814.1}; OS Asparagus officinalis (Garden asparagus). OG Plastid; Chloroplast {ECO:0000313|EMBL:AEX93814.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae; OC Asparagoideae; Asparagus. OX NCBI_TaxID=4686 {ECO:0000313|EMBL:AEX93814.1}; RN [1] {ECO:0000313|EMBL:AEX93814.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22291168; DOI=10.3732/ajb.1100491; RA Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J., RA Pires J.C.; RT "Quality and quantity of data recovered from massively parallel RT sequencing: Examples in Asparagales and Poaceae."; RL Am. J. Bot. 99:330-348(2012). 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 -!- 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; JQ273904; AEX93814.1; -; Genomic_DNA. DR PRIDE; H2F581; -. 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 ECO:0000313|EMBL:AEX93814.1}; 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:AEX93814.1}. 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 480 AA; 53349 MW; 881791255583099F CRC64; MSPQTETKAS VGFKAGVKDY RLTYYTPDYE TKDTDILAAF RVTAQPGVPP EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV IGEAEQFIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFCF CAEALYKAQA ETGEIKGHYL NATAGTCEEM MKRAIFAREL GVPIVMHDYL TGGFTANTTL AHYCRDNGLL LHIHRAMHAV IDRQKNHGMH FRVLAKALRM SGGDHIHAGT VVGKLEGERE MTLGFVDLLR DDYIEKDRSR GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFE PVDKIDKQKV //