ID A3DND9_STAMF Unreviewed; 443 AA. AC A3DND9; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 95. 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=Smar_1051 {ECO:0000313|EMBL:ABN70149.1}; OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Staphylothermus. OX NCBI_TaxID=399550 {ECO:0000313|EMBL:ABN70149.1, ECO:0000313|Proteomes:UP000000254}; RN [1] {ECO:0000313|Proteomes:UP000000254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1 RC {ECO:0000313|Proteomes:UP000000254}; RX PubMed=19341479; DOI=10.1186/1471-2164-10-145; RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., RA Woese C., Bristow J., Kyrpides N.; RT "The complete genome sequence of Staphylothermus marinus reveals RT differences in sulfur metabolism among heterotrophic Crenarchaeota."; RL BMC Genomics 10:145-145(2009). RN [2] {ECO:0000313|EMBL:ABN70149.1, ECO:0000313|Proteomes:UP000000254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1 RC {ECO:0000313|Proteomes:UP000000254}; RX PubMed=21304655; DOI=10.4056/sigs.30527; RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., RA Kyrpides N.C.; RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 RT type strain F1."; RL Stand. Genomic Sci. 1:183-188(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(+) = 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; CP000575; ABN70149.1; -; Genomic_DNA. DR RefSeq; WP_011839340.1; NC_009033.1. DR AlphaFoldDB; A3DND9; -. DR STRING; 399550.Smar_1051; -. DR GeneID; 4906732; -. DR KEGG; smr:Smar_1051; -. DR eggNOG; arCOG04443; Archaea. DR HOGENOM; CLU_031450_3_1_2; -. DR OrthoDB; 52787at2157; -. DR Proteomes; UP000000254; 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, ECO:0000313|EMBL:ABN70149.1}; 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:UP000000254}. FT DOMAIN 11..131 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 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; 49740 MW; C5D759EF6DED7861 CRC64; MPHKFEPYHS YIDKNYVPDL ENDIIAVFRI KPAKGFTIED AAGGVAAESS TGTWTTLYPW YNTERVRKLS GKAYYFKDLG DGSWIVRIAY PVELFEEANM PGLLASIAGN VFGMKRVEGL RLEDIYLPKK FLQYFKGPSK GVEGVKKIFR VTDRPIVGTV PKPKVGYSPE EVEKLAYELL VGGMDYIKDD ENLTSPSFCR FSERAKHIMR AIDRAEKETG ERKVWFANIT SDIREMEKRL KLVADYDNPY VMVDVVVTGW STLTYIRDLA EEYGLAIHAH RAMHAAFTRN PYHGISMYVL AKLYRIIGVD QLHIGTAGVG KLEGGKIDVI RYARILREKH FKPDPDDVFH IEQEMYHIKP AMPVSSGGLH PGNLPGVIDA LGTELVLQIG GGVLGHPDGP RAGAMAVRQS LEAILKGIPL DEYAKTHREL ARALEKWGFA KPI //