ID B7R258_9EURY Unreviewed; 444 AA. AC B7R258; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 24-JAN-2024, entry version 70. 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 ORFNames=TAM4_1764 {ECO:0000313|EMBL:EEB74397.1}; OS Thermococcus sp. AM4. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74397.1, ECO:0000313|Proteomes:UP000009277}; RN [1] {ECO:0000313|EMBL:EEB74397.1, ECO:0000313|Proteomes:UP000009277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM4 {ECO:0000313|EMBL:EEB74397.1, RC ECO:0000313|Proteomes:UP000009277}; RX PubMed=22123768; DOI=10.1128/JB.06259-11; RA Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A., Bartlett D.H., RA Bonch-Osmolovskaya E.A., Lebedinsky A.V.; RT "Complete Genome Sequence of the Hyperthermophilic Archaeon Thermococcus RT sp. Strain AM4, Capable of Organotrophic Growth and Growth at the Expense RT of Hydrogenogenic or Sulfidogenic Oxidation of Carbon Monoxide."; RL J. Bacteriol. 193:7019-7020(2011). 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; CP002952; EEB74397.1; -; Genomic_DNA. DR RefSeq; WP_014122283.1; NC_016051.1. DR AlphaFoldDB; B7R258; -. DR STRING; 246969.TAM4_1764; -. DR GeneID; 7419691; -. DR KEGG; tha:TAM4_1764; -. DR eggNOG; arCOG04443; Archaea. DR HOGENOM; CLU_031450_3_1_2; -. DR OrthoDB; 52787at2157; -. DR Proteomes; UP000009277; 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 3: Inferred from homology; KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01133}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01133}; 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}. FT DOMAIN 12..130 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 142..438 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 163 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT ACT_SITE 281 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 165 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 189 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 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 192 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 282 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 314 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 367..369 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 389..392 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT SITE 322 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT MOD_RES 189 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" SQ SEQUENCE 444 AA; 49807 MW; 8BD0A123C21ED7CB CRC64; MVEKFDKIYD YYVDKGYEPN KKRDIIAVFR VTPAEGYTIE AAAGAVAAES STGTWTTLYP WYEQERWADL SAKAYDFIDM GDGSWIVRIA YPFHAFEEWN LPGLLASIAG NVFGMKRVKG LRLEDLYIPE IVLRNFNGPA FGIEGVRKML EIYDRPLYGV VPKPKVGYSP EEFEKLAYEL LSNGADYMKD DENLTSPWYN RFDERAEIVA RVIDKVENET GEKKTWFANI TADVREMERR LEILADLGLK HAMVDVVITG WGALEYIRDL AADYGLAIHG HRAMHAAFTR NKYHGISMFV LAKLYRIIGI DQLHVGTAGA GKLEGGKWDV IQNARILREE TYTPDENDVF HLEQKFYGMK PAFPTSSGGL HPGNIEPVIE ALGKDIVLQL GGGTLGHPDG PGAGARAVRQ AIDAIMQGIP LDEYAKTHKE LARALEKWGH VTPV //