ID O98949_9RHOD Unreviewed; 493 AA. AC O98949; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 11-NOV-2015, entry version 85. DE SubName: Full=Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit {ECO:0000313|EMBL:BAA75796.1}; OS Galdieria partita. OG Plastid; Chloroplast {ECO:0000313|EMBL:BAA75796.1}. OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; OC Galdieria. OX NCBI_TaxID=83374 {ECO:0000313|EMBL:BAA75796.1}; RN [1] {ECO:0000313|EMBL:BAA75796.1} 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] {ECO:0000213|PDB:1BWV} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND RP CARBOXYLATION AT LYS-210. RX PubMed=10336462; DOI=10.1074/jbc.274.22.15655; RA Sugawara H., Yamamoto H., Shibata N., Inoue T., Okada S., Miyake C., RA Yokota A., Kai Y.; RT "Crystal structure of carboxylase reaction-oriented ribulose 1, 5- RT bisphosphate carboxylase/oxygenase from a thermophilic red alga, RT Galdieria partita."; RL J. Biol. Chem. 274:15655-15661(1999). RN [3] {ECO:0000213|PDB:1IWA} RP X-RAY CRYSTALLOGRAPHY (2.60 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). CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000256|RuleBase:RU000303}. 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; 2.40 A; A/C/E/G=1-493. DR PDB; 1IWA; X-ray; 2.60 A; A/C/E/G/I/K/M/O=1-493. DR ProteinModelPortal; O98949; -. DR SMR; O98949; 14-486. DR EvolutionaryTrace; O98949; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.110; -; 1. DR Gene3D; 3.30.70.150; -; 1. DR HAMAP; MF_01338; RuBisCO_L_type1; 1. DR InterPro; IPR020878; RuBisCo_large_chain_AS. DR InterPro; IPR020888; RuBisCO_lsu. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SUPFAM; SSF51649; SSF51649; 1. DR SUPFAM; SSF54966; SSF54966; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1BWV, ECO:0000213|PDB:1IWA}; KW Chloroplast {ECO:0000256|RuleBase:RU000303, KW ECO:0000313|EMBL:BAA75796.1}; Magnesium {ECO:0000213|PDB:1BWV}; KW Metal-binding {ECO:0000213|PDB:1BWV}; KW Photosynthesis {ECO:0000256|RuleBase:RU004237}; KW Plastid {ECO:0000313|EMBL:BAA75796.1}. FT METAL 210 210 Magnesium. {ECO:0000213|PDB:1BWV}. FT METAL 212 212 Magnesium. {ECO:0000213|PDB:1BWV}. FT METAL 213 213 Magnesium. {ECO:0000213|PDB:1BWV}. FT MOD_RES 210 210 N6-carboxylysine. {ECO:0000213|PDB:1BWV}. 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 //