ID P72383_9FIRM Unreviewed; 479 AA. AC P72383; DT 01-FEB-1997, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 2. DT 27-MAR-2024, entry version 100. DE RecName: Full=ribulose-bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00012287}; DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287}; OS Sulfobacillus acidophilus. OC Bacteria; Bacillota; Clostridia; Eubacteriales; OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus. OX NCBI_TaxID=53633 {ECO:0000313|EMBL:AAB17673.2}; RN [1] {ECO:0000313|EMBL:AAB17673.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAL {ECO:0000313|EMBL:AAB17673.2}; RA Clark D.A., Norris P.R.; RT "Partial sequence of the Rubisco large chain of two acidophilic Gram RT positive, mineral sulphide-oxidising bacteria."; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAB17673.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAL {ECO:0000313|EMBL:AAB17673.2}; RA Caldwell P.E., Norris P.R.; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AAB17673.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NAL {ECO:0000313|EMBL:AAB17673.2}; RX PubMed=17600067; DOI=10.1099/mic.0.2007/006262-0; RA Caldwell P.E., McLean M.R., Norris P.R.; RT "Ribulose bisphosphate carboxylase activity and a Calvin cycle gene cluster RT in Sulfobacillus species."; RL Microbiology 153:2231-2240(2007). 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; U75301; AAB17673.2; -; Genomic_DNA. DR AlphaFoldDB; P72383; -. DR OMA; IHGHPDG; -. 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: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 Calvin cycle {ECO:0000256|ARBA:ARBA00022567}; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 22..141 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 151..458 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" SQ SEQUENCE 479 AA; 53094 MW; 57040D702FF247F7 CRC64; MTTEENKNRW AAGVTPYSKM GYWQPDYQPK DTDILCAFRF VPQEGVDPEE AAAAVAGESS TATWTVVWTD RLTAHEHYQA KAYRVVPVPG TDQYIAYIAY DLDLFEEGSI ANLTASIIGN VFGFKALKSL RLEDMRIPPH YVKTFQGPAH GIVMEREYLN KYGRPLLGAT VKPKLGLSAR NYARVVYEAL RGGLDFTKDD ENINSQPFMR WRDRYLFVME AVNKATADTG EIKGHYLNVT AATMEDIYER ADFAKQIGSP IIMIDLIVGY TAIQSIAKWA RKNGVLLHLH RAGHSTYTRQ KTHGVSFRVI AKWMRLAGVD HIHAGTVLGK LEGDPRTTAG YYQTLRGMKY DADPTIGLYF EQDWASLPGV MPVASGGIHA GQMHQLIDLL GEDVVLQFGG GTFGHPHGIA AGAAANRIAC EAIIQARNEG RDYVNEGPEI LAEAAKWSPA LRAALDTWKD VTFNFESTDT PDVLPTPSF //