ID RBL2_RHOPA Reviewed; 461 AA. AC Q6N0W9; Q8GJP8; Q93TJ8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01339}; DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01339}; DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01339}; GN Name=cbbM {ECO:0000255|HAMAP-Rule:MF_01339}; GN OrderedLocusNames=RPA4641; OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=258594; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DH; RX PubMed=12900023; DOI=10.1016/s0378-1097(03)00482-8; RA Du C., Zhou J., Wang J., Yan B., Lu H., Hou H.; RT "Construction of a genetically engineered microorganism for CO2 fixation RT using a Rhodopseudomonas/Escherichia coli shuttle vector."; RL FEMS Microbiol. Lett. 225:69-73(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DCP3; RX PubMed=15259271; DOI=10.1007/s00248-003-1028-5; RA Oda Y., Meijer W.G., Gibson J.L., Gottschal J.C., Forney L.J.; RT "Analysis of diversity among 3-chlorobenzoate-degrading strains of RT Rhodopseudomonas palustris."; RL Microb. Ecol. 47:68-79(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-98 / CGA009; RX PubMed=14704707; DOI=10.1038/nbt923; RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., RA Harrison F.H., Gibson J., Harwood C.S.; RT "Complete genome sequence of the metabolically versatile photosynthetic RT bacterium Rhodopseudomonas palustris."; RL Nat. Biotechnol. 22:55-61(2004). 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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01339}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01339}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01339}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01339}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type II CC subfamily. {ECO:0000255|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; AY155466; AAN52766.1; -; Genomic_DNA. DR EMBL; AF355197; AAK39106.1; -; Genomic_DNA. DR EMBL; BX572607; CAE30081.1; -; Genomic_DNA. DR RefSeq; WP_011160173.1; NZ_CP116810.1. DR PDB; 4LF1; X-ray; 2.38 A; A/B/C/D/E/F=1-461. DR PDB; 4LF2; X-ray; 2.38 A; A/B/C/D/E/F=1-461. DR PDB; 5HAN; X-ray; 2.04 A; A/B/C/D/E/F/G/H/I/J/K/L=1-461. DR PDB; 5HAO; X-ray; 2.18 A; A/B/C/D/E/F=1-461. DR PDB; 5HAT; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-461. DR PDB; 5HJX; X-ray; 1.80 A; A/B/C/D/E/F=1-461. DR PDB; 5HJY; X-ray; 2.30 A; A/B/C/D/E/F=1-461. DR PDB; 5HK4; X-ray; 2.15 A; A/B/C/D/E/F=1-461. DR PDB; 5HQL; X-ray; 2.53 A; A/B/C/D/E/F=1-461. DR PDB; 5HQM; X-ray; 1.95 A; A/B=1-456. DR PDB; 5KOZ; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-461. DR PDBsum; 4LF1; -. DR PDBsum; 4LF2; -. DR PDBsum; 5HAN; -. DR PDBsum; 5HAO; -. DR PDBsum; 5HAT; -. DR PDBsum; 5HJX; -. DR PDBsum; 5HJY; -. DR PDBsum; 5HK4; -. DR PDBsum; 5HQL; -. DR PDBsum; 5HQM; -. DR PDBsum; 5KOZ; -. DR AlphaFoldDB; Q6N0W9; -. DR SMR; Q6N0W9; -. DR STRING; 258594.RPA4641; -. DR GeneID; 66895793; -. DR eggNOG; COG1850; Bacteria. DR HOGENOM; CLU_031450_3_1_5; -. DR PhylomeDB; Q6N0W9; -. DR Proteomes; UP000001426; 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; 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 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 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 1: Evidence at protein level; KW 3D-structure; Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; KW Metal-binding; Monooxygenase; Oxidoreductase; Photosynthesis; KW Reference proteome. FT CHAIN 1..461 FT /note="Ribulose bisphosphate carboxylase" FT /id="PRO_0000062665" FT ACT_SITE 167 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT ACT_SITE 288 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 112 FT /ligand="substrate" FT /note="in homodimeric partner" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 169 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 192 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 194 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 195 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 289 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT BINDING 369 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT SITE 330 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT MOD_RES 192 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01339" FT CONFLICT 75 FT /note="V -> I (in Ref. 1; AAN52766)" FT /evidence="ECO:0000305" FT CONFLICT 79..80 FT /note="NS -> KG (in Ref. 1; AAN52766)" FT /evidence="ECO:0000305" FT CONFLICT 145 FT /note="K -> R (in Ref. 1; AAN52766)" FT /evidence="ECO:0000305" FT CONFLICT 156 FT /note="I -> V (in Ref. 1; AAN52766)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="A -> S (in Ref. 1; AAN52766)" FT /evidence="ECO:0000305" FT CONFLICT 361 FT /note="M -> L (in Ref. 1; AAN52766)" FT /evidence="ECO:0000305" FT CONFLICT 442..443 FT /note="PQ -> AH (in Ref. 2; AAK39106)" FT /evidence="ECO:0000305" FT HELIX 4..7 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 14..20 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 23..32 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 39..48 FT /evidence="ECO:0007829|PDB:5HJX" FT TURN 49..52 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 63..67 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 71..76 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:5HJX" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 102..109 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 119..128 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 131..134 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 144..151 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 174..185 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:5HQM" FT HELIX 205..223 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 238..252 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 253..258 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 259..264 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 270..279 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:5HJX" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 293..296 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 306..316 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 319..322 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 338..345 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 346..350 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 355..357 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 365..371 FT /evidence="ECO:0007829|PDB:5HJX" FT TURN 374..376 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 377..384 FT /evidence="ECO:0007829|PDB:5HJX" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 394..398 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 404..419 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 424..428 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 432..440 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 442..448 FT /evidence="ECO:0007829|PDB:5HJX" FT HELIX 450..452 FT /evidence="ECO:0007829|PDB:5HJX" SQ SEQUENCE 461 AA; 50485 MW; 907EFB041943AABC CRC64; MDQSNRYANL NLKESELIAG GRHVLCAYIM KPKAGFGNFI QTAAHFAAES STGTNVEVST TDDFTRGVDA LVYEVDEANS LMKIAYPIEL FDRNVIDGRA MIASFLTLTI GNNQGMGDVE YAKMYDFYVP PAYLKLFDGP STTIKDLWRV LGRPVINGGF IVGTIIKPKL GLRPQPFANA CYDFWLGGDF IKNDEPQGNQ VFAPFKDTVR AVADAMRRAQ DKTGEAKLFS FNITADDHYE MLARGEFILE TFADNADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAI AYMITEDAAD GPYFHQEWLG MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH VDGGAAGAKS LRQAEQCWKQ GADPVEFAKD HREFARAFES FPQDADKLYP NWRAKLKPQA A //