RBL2_RHOPA
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 03-AUG-2022, entry version 110.
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}; OrderedLocusNames=RPA4641;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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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; NC_005296.1.
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 PRIDE; Q6N0W9; -.
DR EnsemblBacteria; CAE30081; CAE30081; RPA4641.
DR GeneID; 66895793; -.
DR KEGG; rpa:RPA4641; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_1_5; -.
DR OMA; NQYLHYH; -.
DR PhylomeDB; Q6N0W9; -.
DR BioCyc; RPAL258594:TX73_RS23705-MON; -.
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; -; 1.
DR Gene3D; 3.30.70.150; -; 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; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 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
