ID O98949_9RHOD Unreviewed; 493 AA. AC O98949; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 25-MAY-2022, entry version 116. DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000256|ARBA:ARBA00017725, ECO:0000256|HAMAP-Rule:MF_01338}; DE Short=RuBisCO large subunit {ECO:0000256|HAMAP-Rule:MF_01338}; DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|HAMAP-Rule:MF_01338}; 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; 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:0007829|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, Galdieria RT partita."; RL J. Biol. Chem. 274:15655-15661(1999). RN [3] {ECO:0007829|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 per RT 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: CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5- CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, CC ChEBI:CHEBI:58272; EC=4.1.1.39; CC Evidence={ECO:0000256|ARBA:ARBA00001067, ECO:0000256|HAMAP- CC Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, CC ChEBI:CHEBI:58272; Evidence={ECO:0000256|ARBA:ARBA00000537, CC ECO:0000256|HAMAP-Rule:MF_01338, ECO:0000256|RuleBase:RU000302}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01338, CC ECO:0000256|RuleBase:RU000302}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01338, CC ECO:0000256|RuleBase:RU000302}; CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains. CC {ECO:0000256|ARBA:ARBA00011371, ECO:0000256|HAMAP-Rule:MF_01338, CC 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 RuBisCO CC this homodimer is arranged in a barrel-like tetramer with the small CC subunits forming a tetrameric 'cap' on each end of the 'barrel'. CC {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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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 SMR; O98949; -. DR EvolutionaryTrace; O98949; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule. 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; IPR033966; RuBisCO. DR InterPro; IPR020878; RuBisCo_large_chain_AS. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR036376; RuBisCO_lsu_C_sf. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR InterPro; IPR036422; RuBisCO_lsu_N_sf. DR InterPro; IPR020888; RuBisCO_lsuI. DR PANTHER; PTHR42704; PTHR42704; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDS00014; RuBisCO; 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:0007829|PDB:1BWV, ECO:0007829|PDB:1IWA}; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Chloroplast {ECO:0000256|RuleBase:RU000302, ECO:0000313|EMBL:BAA75796.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01338}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01338}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP- KW Rule:MF_01338}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01338}; 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:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:BAA75796.1}. FT DOMAIN 33..153 FT /note="RuBisCO_large_N" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 164..470 FT /note="RuBisCO_large" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 184 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT ACT_SITE 302 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 210 FT /note="Magnesium" FT /evidence="ECO:0007829|PDB:1BWV" FT METAL 210 FT /note="Magnesium; via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT METAL 212 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338, FT ECO:0007829|PDB:1BWV" FT METAL 213 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338, FT ECO:0007829|PDB:1BWV" FT BINDING 132 FT /note="Substrate; in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 182 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 186 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 303 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 335 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT BINDING 387 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT SITE 342 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338" FT MOD_RES 210 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01338, FT ECO:0007829|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 //