ID RBL_GRATL Reviewed; 488 AA. AC Q6B8P0; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 24-MAR-2009, entry version 32. DE RecName: Full=Ribulose bisphosphate carboxylase large chain; DE Short=RuBisCO large subunit; DE EC=4.1.1.39; GN Name=rbcL; OrderedLocusNames=Grc000164; OS Gracilaria tenuistipitata var. liui (Red alga). OG Plastid; Chloroplast. OC Eukaryota; Rhodophyta; Florideophyceae; Gracilariales; Gracilariaceae; OC Gracilaria. OX NCBI_TaxID=285951; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15638458; DOI=10.1007/s00239-004-2638-3; RA Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., RA de Oliveira M.C.; RT "Comparative analysis of the complete plastid genome sequence of the RT red alga Gracilaria tenuistipitata var. liui provides insights into RT the evolution of rhodoplasts and their relationship to other RT plastids."; RL J. Mol. Evol. 59:464-477(2004). 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 (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose CC 1,5-bisphosphate + CO(2) + H(2)O. CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = CC D-ribulose 1,5-bisphosphate + O(2). CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains CC (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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" (By similarity). CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. 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; AY673996; AAT79745.1; -; Genomic_DNA. DR RefSeq; YP_063670.1; -. DR SMR; Q6B8P0; 10-481. DR GeneID; 2944080; -. DR BRENDA; 4.1.1.39; 302087. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. DR HAMAP; MF_01338; -; 1. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR InterPro; IPR017444; RuBisCO_lsu_N. DR Gene3D; G3DSA:3.20.20.110; RuBisCO_large; 1. DR Gene3D; G3DSA:3.30.70.150; RuBisCO_large; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 3: Inferred from homology; KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium; KW Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration; KW Photosynthesis; Plastid. FT CHAIN 1 488 Ribulose bisphosphate carboxylase large FT chain. FT /FTId=PRO_0000062484. FT ACT_SITE 179 179 Proton acceptor (By similarity). FT ACT_SITE 297 297 Proton acceptor (By similarity). FT METAL 205 205 Magnesium; via carbamate group (By FT similarity). FT METAL 207 207 Magnesium (By similarity). FT METAL 208 208 Magnesium (By similarity). FT BINDING 127 127 Substrate; in homodimeric partner (By FT similarity). FT BINDING 177 177 Substrate (By similarity). FT BINDING 181 181 Substrate (By similarity). FT BINDING 298 298 Substrate (By similarity). FT BINDING 330 330 Substrate (By similarity). FT BINDING 382 382 Substrate (By similarity). FT SITE 337 337 Transition state stabilizer (By FT similarity). FT MOD_RES 205 205 N6-carboxylysine (By similarity). SQ SEQUENCE 488 AA; 54248 MW; 00FC81BA2FD04B80 CRC64; MSQSVEERTR IKNQRYESGV IPYAKMGYWD PNYVVKETDV LALFRVTPQP GVDPVEASAA VAGESSTATW TVVWTDLLTA CDLYRAKAYK VDAVPNTTDQ YFAFIAYDID LFEEGSIANL TASIIGNVFG FKAVKALRLE DMRIPVAYLK TFQGPATGLI VERERMDKFG RPFLGATVKP KLGLSGKNYG RVVYEGLKGG LDFLKDDENI NSQPFMRWKE RFLYSMEAVN RAIAATGETK GHYMNVTAAT MEEMYERAEF AKQLGSIIIM IDLVIGYTAI QTMAIWARKN DMILHLHRAG NSTYSRQKIH GMNFRVICKW MRMSGVDHIH AGTVVGKLEG DPLMIRGFYN TLLQTHLEVN LPQGIFFEQD WASLRKVTPV ASGGIHCGQM HQLLDYLGND VVLQFGGGTI GHPDGIQAGA TANRVALEAM VLARNEGRDY VAEGPQILRD AAKTCGPLQT ALDLWKDITF NYTSTDTADF VETPTANV //