ID RBL2_HYDCU Reviewed; 459 AA. AC Q31IK3; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01339}; DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01339}; DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01339}; DE AltName: Full=Form II RuBisCO {ECO:0000303|PubMed:28115547}; GN Name=cbbM {ECO:0000255|HAMAP-Rule:MF_01339, GN ECO:0000303|PubMed:28115547}; OrderedLocusNames=Tcr_0424; OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira OS crunogena). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales; OC Piscirickettsiaceae; Hydrogenovibrio. OX NCBI_TaxID=317025; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 25203 / XCL-2; RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383; RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A., RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F., RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L., RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M., RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E., RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., RA Tinkham L.E., Zeruth G.T.; RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena RT XCL-2."; RL PLoS Biol. 4:1-17(2006). RN [2] RP INDUCTION. RC STRAIN=DSM 25203 / XCL-2; RX PubMed=28115547; DOI=10.1128/jb.00871-16; RG USF MCB4404L; RA Mangiapia M., Brown T.W., Chaput D., Haller E., Harmer T.L., Hashemy Z., RA Keeley R., Leonard J., Mancera P., Nicholson D., Stevens S., Wanjugi P., RA Zabinski T., Pan C., Scott K.M.; RT "Proteomic and Mutant Analysis of the CO2 Concentrating Mechanism of RT Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena."; RL J. Bacteriol. 199:0-0(2017). 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 at CC the same active site. {ECO:0000255|HAMAP-Rule:MF_01339}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01339}; 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:0000255|HAMAP-Rule:MF_01339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01339}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01339}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01339}. CC -!- INDUCTION: Induced by growth in high levels of dissolved inorganic CC carbon and low NH(3) levels (at protein level). CC {ECO:0000269|PubMed:28115547}. CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large CC chain homodimer in a 'head-to-tail' conformation. In contrast to form I CC RuBisCO, the form II RuBisCO are composed solely of large subunits. CC {ECO:0000255|HAMAP-Rule:MF_01339}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01339}. 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; CP000109; ABB41020.1; -; Genomic_DNA. DR AlphaFoldDB; Q31IK3; -. DR SMR; Q31IK3; -. DR STRING; 317025.Tcr_0424; -. DR KEGG; tcx:Tcr_0424; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_6; -. DR OrthoDB; 9770811at2; -. 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-KW. DR CDD; cd08211; RuBisCO_large_II; 1. DR Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1. DR Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 1. DR HAMAP; MF_01339; RuBisCO_L_type2; 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; IPR020871; RuBisCO_lsuII. DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SFLD; SFLDS00014; RuBisCO; 1. DR SFLD; SFLDG00301; RuBisCO-like_proteins; 1. DR SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1. DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1. DR PROSITE; PS00157; RUBISCO_LARGE; 1. PE 1: Evidence at protein level; KW Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; KW Monooxygenase; Oxidoreductase. FT CHAIN 1..459 FT /note="Ribulose bisphosphate carboxylase" FT /id="PRO_0000251414" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT ACT_SITE 287 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 111 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 193 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 288 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 368 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT SITE 329 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT MOD_RES 191 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" SQ SEQUENCE 459 AA; 50281 MW; CA55D3D2306EA579 CRC64; MDQSNRYADL SLKEEDLIAG QNHILVAYTM EPAAGYGYLE VAAHIAAESS TGTNVEVCTT DDFTKGVDAI VYDIDEANGI MKVAYPFDLF DRNGLDGKTM IVSFLTLAIG NNQGMGDVKN LQMFDFWVPE TKLHLFDGPA VDITNMWKML GRDKDNGGYI AGTIIKPKLG LRPEPFADAA YQFWLGGDFI KNDEPQGNQT FCPMKKVIPL VADAMKRAQD ETGETKLFSA NITADDHHEM CYRADYILET FGADAPQVAF LVDGYVGGPG MITTARRNYP SQYLHYHRAG HGAITSPSAK RGYTAFVLAK ISRLQGASGI HVGTMGYGKM EGDASDKNIA YMIERDECQG PAFYQKWNGM KPTTPIISGG MNALRLPGFF ENLGHGNVIN TSGGGSYGHI DSPAAGATSL RQSYECWKSG ADPIEFAKDH KEFARAFESF PADADKIYPG WREKLGVHK //