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Database: UniProt
Entry: RBL2_RHOPA
LinkDB: RBL2_RHOPA
Original site: 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   05-DEC-2018, entry version 95.
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; Proteobacteria; Alphaproteobacteria; Rhizobiales;
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
RT   fixation 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
RT   photosynthetic 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
CC       at the same active site. {ECO:0000255|HAMAP-Rule:MF_01339}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 3-phospho-D-glycerate + 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 = 2-phosphoglycolate +
CC         3-phospho-D-glycerate + 2 H(+); Xref=Rhea:RHEA:36631,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870,
CC         ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
CC         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-
CC       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
CC       form I RuBisCO, the form II RuBisCO are composed solely of large
CC       subunits. {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}.
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   ProteinModelPortal; Q6N0W9; -.
DR   SMR; Q6N0W9; -.
DR   STRING; 258594.RPA4641; -.
DR   PRIDE; Q6N0W9; -.
DR   EnsemblBacteria; CAE30081; CAE30081; RPA4641.
DR   KEGG; rpa:RPA4641; -.
DR   eggNOG; ENOG4105DT1; Bacteria.
DR   eggNOG; COG1850; LUCA.
DR   HOGENOM; HOG000230831; -.
DR   KO; K01601; -.
DR   OMA; TARRQYP; -.
DR   OrthoDB; POG091H14UZ; -.
DR   PhylomeDB; Q6N0W9; -.
DR   BioCyc; RPAL258594:TX73_RS23705-MONOMER; -.
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;
KW   Complete proteome; Lyase; Magnesium; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Photosynthesis; Reference proteome.
FT   CHAIN         1    461       Ribulose bisphosphate carboxylase.
FT                                /FTId=PRO_0000062665.
FT   ACT_SITE    167    167       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   ACT_SITE    288    288       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   METAL       192    192       Magnesium; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_01339}.
FT   METAL       194    194       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   METAL       195    195       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     112    112       Substrate; in homodimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01339}.
FT   BINDING     169    169       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     289    289       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     322    322       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   BINDING     369    369       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   SITE        330    330       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01339}.
FT   MOD_RES     192    192       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01339}.
FT   CONFLICT     75     75       V -> I (in Ref. 1; AAN52766).
FT                                {ECO:0000305}.
FT   CONFLICT     79     80       NS -> KG (in Ref. 1; AAN52766).
FT                                {ECO:0000305}.
FT   CONFLICT    145    145       K -> R (in Ref. 1; AAN52766).
FT                                {ECO:0000305}.
FT   CONFLICT    156    156       I -> V (in Ref. 1; AAN52766).
FT                                {ECO:0000305}.
FT   CONFLICT    348    348       A -> S (in Ref. 1; AAN52766).
FT                                {ECO:0000305}.
FT   CONFLICT    361    361       M -> L (in Ref. 1; AAN52766).
FT                                {ECO:0000305}.
FT   CONFLICT    442    443       PQ -> AH (in Ref. 2; AAK39106).
FT                                {ECO:0000305}.
FT   HELIX         4      7       {ECO:0000244|PDB:5HJX}.
FT   HELIX        14     20       {ECO:0000244|PDB:5HJX}.
FT   STRAND       23     32       {ECO:0000244|PDB:5HJX}.
FT   HELIX        39     48       {ECO:0000244|PDB:5HJX}.
FT   TURN         49     52       {ECO:0000244|PDB:5HJX}.
FT   HELIX        63     67       {ECO:0000244|PDB:5HJX}.
FT   STRAND       71     76       {ECO:0000244|PDB:5HJX}.
FT   HELIX        77     79       {ECO:0000244|PDB:5HJX}.
FT   STRAND       81     87       {ECO:0000244|PDB:5HJX}.
FT   HELIX        88     90       {ECO:0000244|PDB:5HJX}.
FT   TURN         95     97       {ECO:0000244|PDB:5HJX}.
FT   HELIX       102    109       {ECO:0000244|PDB:5HJX}.
FT   HELIX       112    114       {ECO:0000244|PDB:5HJX}.
FT   STRAND      119    128       {ECO:0000244|PDB:5HJX}.
FT   HELIX       131    134       {ECO:0000244|PDB:5HJX}.
FT   HELIX       144    151       {ECO:0000244|PDB:5HJX}.
FT   STRAND      155    157       {ECO:0000244|PDB:5HJX}.
FT   STRAND      161    165       {ECO:0000244|PDB:5HJX}.
FT   STRAND      167    170       {ECO:0000244|PDB:5HJX}.
FT   HELIX       174    185       {ECO:0000244|PDB:5HJX}.
FT   STRAND      189    192       {ECO:0000244|PDB:5HJX}.
FT   STRAND      198    200       {ECO:0000244|PDB:5HQM}.
FT   HELIX       205    223       {ECO:0000244|PDB:5HJX}.
FT   STRAND      228    232       {ECO:0000244|PDB:5HJX}.
FT   HELIX       238    252       {ECO:0000244|PDB:5HJX}.
FT   HELIX       253    258       {ECO:0000244|PDB:5HJX}.
FT   STRAND      259    264       {ECO:0000244|PDB:5HJX}.
FT   HELIX       265    268       {ECO:0000244|PDB:5HJX}.
FT   HELIX       270    279       {ECO:0000244|PDB:5HJX}.
FT   STRAND      283    288       {ECO:0000244|PDB:5HJX}.
FT   TURN        290    292       {ECO:0000244|PDB:5HJX}.
FT   HELIX       293    296       {ECO:0000244|PDB:5HJX}.
FT   STRAND      302    304       {ECO:0000244|PDB:5HJX}.
FT   HELIX       306    316       {ECO:0000244|PDB:5HJX}.
FT   STRAND      319    322       {ECO:0000244|PDB:5HJX}.
FT   STRAND      328    332       {ECO:0000244|PDB:5HJX}.
FT   HELIX       335    337       {ECO:0000244|PDB:5HJX}.
FT   HELIX       338    345       {ECO:0000244|PDB:5HJX}.
FT   STRAND      346    350       {ECO:0000244|PDB:5HJX}.
FT   STRAND      355    357       {ECO:0000244|PDB:5HJX}.
FT   STRAND      365    371       {ECO:0000244|PDB:5HJX}.
FT   TURN        374    376       {ECO:0000244|PDB:5HJX}.
FT   HELIX       377    384       {ECO:0000244|PDB:5HJX}.
FT   STRAND      389    392       {ECO:0000244|PDB:5HJX}.
FT   HELIX       394    398       {ECO:0000244|PDB:5HJX}.
FT   HELIX       404    419       {ECO:0000244|PDB:5HJX}.
FT   HELIX       424    428       {ECO:0000244|PDB:5HJX}.
FT   HELIX       432    440       {ECO:0000244|PDB:5HJX}.
FT   HELIX       442    448       {ECO:0000244|PDB:5HJX}.
FT   HELIX       450    452       {ECO:0000244|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
//
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