ID D5WV36_KYRT2 Unreviewed; 478 AA. AC D5WV36; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 69. DE RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287}; DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287}; GN OrderedLocusNames=Btus_2871 {ECO:0000313|EMBL:ADG07508.1}; OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae). OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia. OX NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG07508.1, ECO:0000313|Proteomes:UP000002368}; RN [1] {ECO:0000313|Proteomes:UP000002368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., RA Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.; RT "The complete genome of Bacillus tusciae DSM 2912."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADG07508.1, ECO:0000313|Proteomes:UP000002368} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368}; RX PubMed=22180816; DOI=10.4056/sigs.2144922; RA Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M., RA Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L., RA Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A., RA Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C., RA Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V., RA Hugenholtz P., Eisen J.A.; RT "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus RT tusciae type strain (T2) and reclassification in the new genus, Kyrpidia RT gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family RT Alicyclobacillaceae da Costa and Rainey, 2010."; RL Stand. Genomic Sci. 5:121-134(2011). 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}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. CC {ECO:0000256|RuleBase:RU003834}. 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; CP002017; ADG07508.1; -; Genomic_DNA. DR AlphaFoldDB; D5WV36; -. DR STRING; 562970.Btus_2871; -. DR KEGG; bts:Btus_2871; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_2_0_9; -. DR Proteomes; UP000002368; Chromosome. 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:UniProtKB-EC. DR GO; GO:0009086; P:methionine biosynthetic process; 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; 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_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; 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; SFLDG01052; RuBisCO; 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 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167}; KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ADG07508.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 21..140 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 150..457 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" SQ SEQUENCE 478 AA; 53224 MW; 7FA37074DA659678 CRC64; MEQDVKKRWA SGVIPYKEMG YWQPDYEVKD TDVIAAFRVV PQEGIDPEEA AAAVAGESST ATWTVVWTDR LTTYEHYQGK AFRVDPVPGT DQYIAYIAYD IDLFEEGSIA NLASSIIGNV FGFKALKSLR LEDMRIPLHY VKTFQGPAHG IVMEREMLNK YGRPLLGATT KPKLGLSARN YGRVVYEALR GGLDFVKDDE NINSQPFMRW RDRFLYAMEA VHRAMAETGE IKGHYLNVTG ATMEDIYERA EFAKELGSVI VMIDLTVGYS AIQSLAKWAR RNSVLLHLHR AGHSTFTRQK THGVSFRVIA KWMRLAGVDH LHAGTVVGKL EGDPNITKGY YQTLRGMKYD ADPRLGLLFE QDWGSMPAVM PVASGGIHAG QVHQLIDLFG EDVIFQFGGG TIGHPMGIAA GATANRVAIE AMIQARNEGR DILREGPEIL EKAAKWSPEL RAALEVWKDV TFNYASTDTP DVVATPTF //