ID D6CTT0_THIA3 Unreviewed; 461 AA. AC D6CTT0; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 24-JAN-2024, entry version 71. DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000256|ARBA:ARBA00019702, ECO:0000256|HAMAP-Rule:MF_01339}; DE Short=RuBisCO {ECO:0000256|HAMAP-Rule:MF_01339}; DE EC=4.1.1.39 {ECO:0000256|ARBA:ARBA00012287, ECO:0000256|HAMAP-Rule:MF_01339}; GN Name=cbbM {ECO:0000256|HAMAP-Rule:MF_01339, GN ECO:0000313|EMBL:CAZ88699.1}; GN OrderedLocusNames=THI_2041 {ECO:0000313|EMBL:CAZ88699.1}; OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas. OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ88699.1, ECO:0000313|Proteomes:UP000002372}; RN [1] {ECO:0000313|Proteomes:UP000002372} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22701 / CIP 110005 / 3As RC {ECO:0000313|Proteomes:UP000002372}; RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859; RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M., RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V., RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J., RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C., RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P., RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E., RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.; RT "Structure, function, and evolution of the Thiomonas spp. genome."; RL PLoS Genet. 6:E1000859-E1000859(2010). CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide CC fixation, as well as the oxidative fragmentation of the pentose CC substrate. Both reactions occur simultaneously and in competition at CC the same active site. {ECO:0000256|HAMAP-Rule:MF_01339}. 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_01339}; 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_01339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01339}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01339}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01339}. CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large CC chain homodimer in a 'head-to-tail' conformation. In contrast to form I CC RuBisCO, the form II RuBisCO are composed solely of large subunits. CC {ECO:0000256|HAMAP-Rule:MF_01339}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01339}. 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; FP475956; CAZ88699.1; -; Genomic_DNA. DR RefSeq; WP_013106007.1; NZ_CTRL01000038.1. DR AlphaFoldDB; D6CTT0; -. DR KEGG; thi:THI_2041; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_4; -. DR OrthoDB; 9770811at2; -. DR Proteomes; UP000002372; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. DR CDD; cd08211; RuBisCO_large_II; 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_01339; RuBisCO_L_type2; 1. DR InterPro; IPR033966; RuBisCO. 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 InterPro; IPR020871; RuBisCO_lsuII. 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 SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1. DR SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1. PE 3: Inferred from homology; KW Calvin cycle {ECO:0000256|HAMAP-Rule:MF_01339}; KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01339}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01339, ECO:0000313|EMBL:CAZ88699.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01339}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01339}; KW Monooxygenase {ECO:0000256|HAMAP-Rule:MF_01339}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01339}; KW Reference proteome {ECO:0000313|Proteomes:UP000002372}. FT DOMAIN 14..132 FT /note="Ribulose bisphosphate carboxylase large subunit FT ferrodoxin-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF02788" FT DOMAIN 145..442 FT /note="Ribulose bisphosphate carboxylase large subunit C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF00016" FT ACT_SITE 168 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT ACT_SITE 289 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 113 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 170 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 193 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 195 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 290 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 323 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT BINDING 370 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT SITE 331 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" FT MOD_RES 193 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01339" SQ SEQUENCE 461 AA; 50819 MW; 15B9E0F51FEAA8D3 CRC64; MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE SSTGTNVEVS TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR FMIVSFLTLV IGNNQGMGDV EYGKMIDFYV PERAIQMFDG PATDISNLWR ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ AAYQFWLGGD FIKNDEPQGN QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH EMCARADFAL EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC QGPVYYQKWY GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG HIDSPAAGAK SLRQAYECWK AGADPIEYAK EHIEFARAFE SFPGDADKLF PGWRDKLGVH K //