ID O98949_9RHOD Unreviewed; 493 AA. AC O98949; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 02-NOV-2016, entry version 94. 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: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 -!- 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 -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains. CC {ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}. 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 -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I CC subfamily. {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; 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 PDBsum; 1BWV; -. DR PDBsum; 1IWA; -. DR ProteinModelPortal; O98949; -. DR SMR; O98949; -. DR EvolutionaryTrace; O98949; -. 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; 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 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 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:BAA75796.1}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Magnesium {ECO:0000213|PDB:1BWV, ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; KW Metal-binding {ECO:0000213|PDB:1BWV, ECO:0000256|HAMAP-Rule:MF_01338, KW ECO:0000256|RuleBase:RU000302}; 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:BAA75796.1}. FT DOMAIN 33 153 RuBisCO_large_N. {ECO:0000259|Pfam: FT PF02788}. FT DOMAIN 164 470 RuBisCO_large. {ECO:0000259|Pfam: FT PF00016}. FT ACT_SITE 184 184 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT ACT_SITE 302 302 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT METAL 210 210 Magnesium. {ECO:0000213|PDB:1BWV}. FT METAL 210 210 Magnesium; via carbamate group. FT {ECO:0000256|HAMAP-Rule:MF_01338}. FT METAL 212 212 Magnesium. {ECO:0000213|PDB:1BWV, FT ECO:0000256|HAMAP-Rule:MF_01338}. FT METAL 213 213 Magnesium. {ECO:0000213|PDB:1BWV, FT ECO:0000256|HAMAP-Rule:MF_01338}. FT BINDING 132 132 Substrate; in homodimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01338}. FT BINDING 182 182 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 186 186 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 303 303 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 335 335 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT BINDING 387 387 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01338}. FT SITE 342 342 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01338}. FT MOD_RES 210 210 N6-carboxylysine. {ECO:0000213|PDB:1BWV, FT ECO:0000256|HAMAP-Rule:MF_01338}. 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 //