ID D3RYU4_FERPA Unreviewed; 443 AA. AC D3RYU4; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 76. 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=Ferp_1506 {ECO:0000313|EMBL:ADC65657.1}; OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; OC Ferroglobus. OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC65657.1, ECO:0000313|Proteomes:UP000002613}; RN [1] {ECO:0000313|Proteomes:UP000002613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D., RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.; RT "Complete sequence of Ferroglobus placidus DSM 10642."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADC65657.1, ECO:0000313|Proteomes:UP000002613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613}; RX PubMed=22180810; DOI=10.4056/sigs.2225018; RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A., RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T., RA Lovley D., Kyrpides N., Ivanova N.; RT "Complete genome sequence of Ferroglobus placidus AEDII12DO."; RL Stand. Genomic Sci. 5:50-60(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; CP001899; ADC65657.1; -; Genomic_DNA. DR RefSeq; WP_012965998.1; NC_013849.1. DR AlphaFoldDB; D3RYU4; -. DR STRING; 589924.Ferp_1506; -. DR PaxDb; 589924-Ferp_1506; -. DR GeneID; 8779026; -. DR KEGG; fpl:Ferp_1506; -. DR eggNOG; arCOG04443; Archaea. DR HOGENOM; CLU_031450_3_1_2; -. DR OrthoDB; 52787at2157; -. DR Proteomes; UP000002613; 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01133, ECO:0000313|EMBL:ADC65657.1}; 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:UP000002613}. FT DOMAIN 12..130 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 141..437 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT COILED 198..246 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 162 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT ACT_SITE 280 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 164 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 188 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 190 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" 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 281 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 313 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 366..368 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 388..391 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT SITE 321 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT MOD_RES 188 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" SQ SEQUENCE 443 AA; 50008 MW; 0C8405ED8D8D00A3 CRC64; MAERYGEIYD YYVDESYEPN RKRDVIAVFK ITPAEGYTIK ECAGGVAAES STGTWTTLYP WYEEERWKDL SAKAYEFVEH DGSWIVKIAY PYHAFEERNL PALLASIAGN VFGMRRVKAL RLEDLYLPEK LIREFKGPSK GIEGVRKMLE IKDRPIYGVV PKPKVGYSAE EFESLAYDLL SSGADYIKDD ENLASPWYNR FEERARIVSR VIEKVESETG EKKTWFANIT ANVKEMERRL EILAEHNLKH AMVDVVICGW AVLEHIRDIA EDYNLAIHGH RAMHAAFTRN PQHGISMFVL AKLYRLIGID QLHVGTAGAG KLEGGKWEVI QNARILREMH YKPEEGDVFH LEQKFYSIKP AFPVSSGGLH PGNLAQVFEA LGTDIVIQVG GGTVGHPDGP KAGAKAVRQA IDAIMQGIPL EEYAKKHKEL ARALEKWGTV TPI //