ID O98949_9RHOD Unreviewed; 493 AA. AC O98949; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 16-DEC-2008, entry version 46. DE RecName: Full=Ribulose bisphosphate carboxylase large chain; DE EC=4.1.1.39; 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.; RT "Structure and function study of ribulose-1,5-bisphosphate RT carboxylase/oxygenase of the red algae, Galdieria partita Tokara."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=22209281; 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 MEDLINE=97059078; 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 -!- 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 -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains CC (By similarity). CC -!- SUBCELLULAR LOCATION: Plastid, 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 GO; GO:0009573; C:chloroplast ribulose bisphosphate carboxyla...; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW Chloroplast; Plastid. 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 //