ID A2BK54_HYPBU Unreviewed; 441 AA. AC A2BK54; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 87. DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|HAMAP-Rule:MF_01133}; DE Short=RuBisCO {ECO:0000256|HAMAP-Rule:MF_01133}; DE EC=4.1.1.39 {ECO:0000256|HAMAP-Rule:MF_01133}; GN Name=rbcL {ECO:0000256|HAMAP-Rule:MF_01133}; GN OrderedLocusNames=Hbut_0503 {ECO:0000313|EMBL:ABM80365.1}; OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae; OC Hyperthermus. OX NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM80365.1, ECO:0000313|Proteomes:UP000002593}; RN [1] {ECO:0000313|EMBL:ABM80365.1, ECO:0000313|Proteomes:UP000002593} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5 RC {ECO:0000313|Proteomes:UP000002593}; RX PubMed=17350933; RA Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., RA She Q., Garrett R.A., Klenk H.P.; RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."; RL Archaea 2:127-135(2007). RN [2] {ECO:0007829|PDB:6HUN} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS). RX PubMed=31205016; DOI=10.1107/S2059798319006466; RA Bundela R., Keown J., Watkin S., Pearce F.G.; RT "Structure of a hyperthermostable dimeric archaeal Rubisco from RT Hyperthermus butylicus."; RL Acta Crystallogr. D Struct. Biol. 75:536-544(2019). CC -!- FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to CC ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3- CC phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation CC pathway, together with AMP phosphorylase and R15P isomerase. CC {ECO:0000256|HAMAP-Rule:MF_01133}. 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:0000256|HAMAP- CC Rule:MF_01133}; 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|HAMAP-Rule:MF_01133}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01133}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01133}; CC -!- SUBUNIT: Homodimer or homodecamer. In contrast to form I RuBisCO, the CC form III RuBisCO is composed solely of large subunits. CC {ECO:0000256|HAMAP-Rule:MF_01133}. CC -!- MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO are CC all anaerobic, it is most likely that only the carboxylase activity of CC RuBisCO, and not the competitive oxygenase activity (by which RuBP CC reacts with O(2) to form one molecule of 3-phosphoglycerate and one CC molecule of 2-phosphoglycolate), is biologically relevant in these CC strains. {ECO:0000256|HAMAP-Rule:MF_01133}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01133}. 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; CP000493; ABM80365.1; -; Genomic_DNA. DR RefSeq; WP_011821683.1; NC_008818.1. DR PDB; 6HUN; X-ray; 1.80 A; A=1-441. DR PDBsum; 6HUN; -. DR AlphaFoldDB; A2BK54; -. DR SMR; A2BK54; -. DR STRING; 415426.Hbut_0503; -. DR EnsemblBacteria; ABM80365; ABM80365; Hbut_0503. DR GeneID; 4781477; -. DR KEGG; hbu:Hbut_0503; -. DR eggNOG; arCOG04443; Archaea. DR HOGENOM; CLU_031450_3_1_2; -. DR OrthoDB; 52787at2157; -. DR Proteomes; UP000002593; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW. DR CDD; cd08213; RuBisCO_large_III; 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_01133; RuBisCO_L_type3; 1. DR InterPro; IPR033966; RuBisCO. DR InterPro; IPR017712; RuBisCO_III. 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 NCBIfam; TIGR03326; rubisco_III; 1. 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; 2. 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. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:6HUN}; KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01133, ECO:0000313|EMBL:ABM80365.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01133}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01133}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01133}; KW Reference proteome {ECO:0000313|Proteomes:UP000002593}. FT DOMAIN 11..129 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 139..435 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 160 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT ACT_SITE 278 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 162 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 186 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 188 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 189 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 279 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 311 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 364..366 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 386..389 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT SITE 319 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT MOD_RES 186 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" SQ SEQUENCE 441 AA; 49178 MW; F8A627C6D6189C16 CRC64; MHEHFDSIYL EFVDESYKPG KDEVIAVFRV TPAQGISIKD AAGRIAAESS VGTWTTLSVK PSWFEKLKAK AYRFHDLGDG SWLVWVAYPV ELFEEGSIPN FASSILGNIF GMKAIAGLRV EDVYFPPSYL ETFPGPNKGI QGVREILGIK DRPILATVPK PKLGYTPEEY GRVAYEILIG GIDLVKDDEN FASQPFCRFE ARLKEVMKAI DRAEKETGER KGYLANVTAP IREMEKRIKL VADYGNKFIM IDFLTAGWAA LQHARELAEE YDLAIHGHRA FHAAFTRNPK HGVSMFLVAK LARMAGVDHV HVGTPGVGKM DAKTREVLEH TRIVREQYYR PKEGDLFHLE QPWSNIKPVF PVASGGLHPG TLPEVIRVMG KDIIMQVGGG VLGHPDGPEA GARAVRQAVE AAMKGISLDE YAREHRELAR ALEKWGYVRP V //