ID O98949_9RHOD PRELIMINARY; PRT; 493 AA. AC O98949; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 30-MAY-2006, entry version 29. DE Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit. GN Name=rbcL; OS Galdieria partita. OG Plastid; Chloroplast. OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; OC Galdieria. OX NCBI_TaxID=83374; RN [1] RP NUCLEOTIDE SEQUENCE. RA Tomizawa K.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=12220629; DOI=10.1016/S0014-5793(02)03148-4; RA Okano Y., Mizohata E., Xie Y., Matsumura H., Sugawara H., Inoue T., RA Yokota A., Kai Y.; RT "X-ray structure of Galdieria Rubisco complexed with one sulfate ion RT per active site."; RL FEBS Lett. 527:33-36(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=8900108; DOI=10.1074/jbc.271.43.26449; RA Shibata N., Inoue T., Fukuhara K., Nagara Y., Kitagawa R., Harada S., RA Kasai N., Uemura K., Kato K., Yokota A., Kai Y.; RT "Orderly disposition of heterogeneous small subunits in D-ribulose- RT 1,5-bisphosphate carboxylase/oxygenase from spinach."; RL J. Biol. Chem. 271:26449-26452(1996). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: D-ribulose 1,5-bisphosphate + CO(2) + H(2)O = CC 2 3-phospho-D-glycerate + 2 H(+). CC -!- CATALYTIC ACTIVITY: D-ribulose 1,5-bisphosphate + O(2) = 3- CC phospho-D-glycerate + 2-phosphoglycolate. CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains CC (By similarity). CC -!- SUBCELLULAR LOCATION: Chloroplast (By similarity). CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. 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; AB018008; BAA75796.1; -; Genomic_DNA. DR PDB; 1BWV; X-ray; A/C/E/G=1-493. DR PDB; 1IWA; X-ray; A/C/E/G/I/K/M/O=1-493. DR GO; GO:0009507; C:chloroplast; IEA. DR GO; GO:0009573; C:ribulose bisphosphate carboxylase complex (...; IEA. DR GO; GO:0016829; F:lyase activity; IEA. DR GO; GO:0004497; F:monooxygenase activity; IEA. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA. DR GO; GO:0015979; P:photosynthesis; IEA. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA. DR InterPro; IPR000685; RuBisCO_large. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. KW Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; KW Monooxygenase; Oxidoreductase; Photosynthesis. SQ SEQUENCE 493 AA; 54994 MW; FF86E3FF8C68C937 CRC64; MSQSIEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR VTPQPGVDPI EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP NNPEQYFAYI AYELDLFEEG SIANLTASII GNVFGFKAVK ALRLEDMRLP LAYLKTFQGP ATGVILERER LDKFGRPLLG CTTKPKLGLS GKNYGRVVYE ALKGGLDFVK DDENINSQPF MRWRERYLFT MEAVNKASAA TGEVKGHYLN VTAATMEEMY ARANFAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT RGFYKTLLLP KLERNLQEGL FFDMEWASLR KVMPVASGGI HAGQMHQLIH YLGEDVVLQF GGGTIGHPDG IQAGATANRV ALEAMILARN ENRDYLTEGP EILREAAKTC GALRTALDLW KDITFNYTST DTSDFVETPT ANI //