ID A3CV55_METMJ Unreviewed; 430 AA. AC A3CV55; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 02-SEP-2026, entry version 105. 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=Memar_1325 {ECO:0000313|EMBL:ABN57255.1}; OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanomicrobiales; Methanomicrobiaceae; Methanoculleus. OX NCBI_TaxID=368407 {ECO:0000313|EMBL:ABN57255.1, ECO:0000313|Proteomes:UP000002146}; RN [1] {ECO:0000313|EMBL:ABN57255.1, ECO:0000313|Proteomes:UP000002146} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35101 / DSM 1498 / JR1 RC {ECO:0000313|Proteomes:UP000002146}; RX PubMed=21304656; DOI=10.4056/sigs.32535; RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.; RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 RT type strain JR1."; RL Stand. Genomic Sci. 1:189-196(2009). 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(+) = D-ribulose 1,5- CC bisphosphate + CO2 + 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, ECO:0000256|PROSITE-ProRule:PRU10114}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribulose 1,5-bisphosphate + O2 = 2-phosphoglycolate + (2R)- CC 3-phosphoglycerate + 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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; CP000562; ABN57255.1; -; Genomic_DNA. DR RefSeq; WP_011844166.1; NC_009051.1. DR AlphaFoldDB; A3CV55; -. DR STRING; 368407.Memar_1325; -. DR GeneID; 4848035; -. DR GeneID; 76729398; -. DR KEGG; mem:Memar_1325; -. DR eggNOG; arCOG04443; Archaea. DR HOGENOM; CLU_031450_3_1_2; -. DR OrthoDB; 52787at2157; -. DR Proteomes; UP000002146; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. 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:InterPro. 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; 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 NCBIfam; NF003252; PRK04208.1; 1. DR NCBIfam; TIGR03326; rubisco_III; 1. DR PANTHER; PTHR42704; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1. DR PANTHER; PTHR42704:SF17; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 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 Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_01133}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01133}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01133}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01133}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01133}; Reference proteome {ECO:0000313|Proteomes:UP000002146}. FT DOMAIN 8..121 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 133..424 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 152 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT ACT_SITE 270 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 178 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 180 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133, FT ECO:0000256|PROSITE-ProRule:PRU10114" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 271 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 303 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT BINDING 353..355 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT SITE 310 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133" FT MOD_RES 178 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01133, FT ECO:0000256|PROSITE-ProRule:PRU10114" SQ SEQUENCE 430 AA; 47331 MW; 08D87E9C4B244477 CRC64; MAIDWYEEFV DLNHTPGPDE LVALYYFEPA AGISKEEAVG RIASESSTGT WTTLFTLPPR MRDLQAKAFE IEGNYVKIAY PLALWEEGNA AQLLSGIAGN VFGMKALDRL RLIDASLPAE YLRHFKGPHF GMEGIRDMMK IRGRPLTGAV PKPKVGFTAE EHAEVGYETW MGGFDFVKDD ENLTSQSFNR FDDRVRAMAK MRDRAEQETG DVKSAFINIT ADTETMEKRA KMLADYGWNY AMIDVVVAGT AAVATLRDYC SDLGLAIHAH RAMHAAFDRD EKHGITMQFL AKMMRLVGVA QIHTGTAVGK LVGTRAEATV LADMLREKHT NAVDHMALDQ DWGNIKSAFP VSSGGLHPGL VPDVLDIYGS ELVLLVSGGI HGHPKGTRAG AEAAMQAIEA WKEGETLEEK AKKAPALSEA LEKWGRYKPK //