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Q6N0W9

- RBL2_RHOPA

UniProt

Q6N0W9 - RBL2_RHOPA

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Protein
Ribulose bisphosphate carboxylase
Gene
cbbM, RPA4641
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site By similarity.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121Substrate; in homodimeric partner By similarity
Active sitei167 – 1671Proton acceptor By similarity
Binding sitei169 – 1691Substrate By similarity
Metal bindingi192 – 1921Magnesium; via carbamate group By similarity
Metal bindingi194 – 1941Magnesium By similarity
Metal bindingi195 – 1951Magnesium By similarity
Active sitei288 – 2881Proton acceptor By similarity
Binding sitei289 – 2891Substrate By similarity
Binding sitei322 – 3221Substrate By similarity
Sitei330 – 3301Transition state stabilizer By similarity
Binding sitei369 – 3691Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:cbbM
Ordered Locus Names:RPA4641
OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Taxonomic identifieri258594 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001426: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Ribulose bisphosphate carboxylaseUniRule annotation
PRO_0000062665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-carboxylysine By similarity

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi258594.RPA4641.

Structurei

3D structure databases

ProteinModelPortaliQ6N0W9.
SMRiQ6N0W9. Positions 2-456.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiAKEHREF.
OrthoDBiEOG66QKT8.
PhylomeDBiQ6N0W9.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6N0W9-1 [UniParc]FASTAAdd to Basket

« Hide

MDQSNRYANL NLKESELIAG GRHVLCAYIM KPKAGFGNFI QTAAHFAAES    50
STGTNVEVST TDDFTRGVDA LVYEVDEANS LMKIAYPIEL FDRNVIDGRA 100
MIASFLTLTI GNNQGMGDVE YAKMYDFYVP PAYLKLFDGP STTIKDLWRV 150
LGRPVINGGF IVGTIIKPKL GLRPQPFANA CYDFWLGGDF IKNDEPQGNQ 200
VFAPFKDTVR AVADAMRRAQ DKTGEAKLFS FNITADDHYE MLARGEFILE 250
TFADNADHIA FLVDGYVAGP AAVTTARRAF PKQYLHYHRA GHGAVTSPQS 300
KRGYTAFVLS KMARLQGASG IHTGTMGFGK MEGEAADRAI AYMITEDAAD 350
GPYFHQEWLG MNPTTPIISG GMNALRMPGF FDNLGHSNLI MTAGGGAFGH 400
VDGGAAGAKS LRQAEQCWKQ GADPVEFAKD HREFARAFES FPQDADKLYP 450
NWRAKLKPQA A 461
Length:461
Mass (Da):50,485
Last modified:July 5, 2004 - v1
Checksum:i907EFB041943AABC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751V → I in AAN52766. 1 Publication
Sequence conflicti79 – 802NS → KG in AAN52766. 1 Publication
Sequence conflicti145 – 1451K → R in AAN52766. 1 Publication
Sequence conflicti156 – 1561I → V in AAN52766. 1 Publication
Sequence conflicti348 – 3481A → S in AAN52766. 1 Publication
Sequence conflicti361 – 3611M → L in AAN52766. 1 Publication
Sequence conflicti442 – 4432PQ → AH in AAK39106. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY155466 Genomic DNA. Translation: AAN52766.1.
AF355197 Genomic DNA. Translation: AAK39106.1.
BX572607 Genomic DNA. Translation: CAE30081.1.
RefSeqiNP_949975.1. NC_005296.1.
WP_011160173.1. NC_005296.1.

Genome annotation databases

EnsemblBacteriaiCAE30081; CAE30081; RPA4641.
GeneIDi2692140.
KEGGirpa:RPA4641.
PATRICi23293933. VBIRhoPal84835_4873.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY155466 Genomic DNA. Translation: AAN52766.1 .
AF355197 Genomic DNA. Translation: AAK39106.1 .
BX572607 Genomic DNA. Translation: CAE30081.1 .
RefSeqi NP_949975.1. NC_005296.1.
WP_011160173.1. NC_005296.1.

3D structure databases

ProteinModelPortali Q6N0W9.
SMRi Q6N0W9. Positions 2-456.
ModBasei Search...

Protein-protein interaction databases

STRINGi 258594.RPA4641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE30081 ; CAE30081 ; RPA4641 .
GeneIDi 2692140.
KEGGi rpa:RPA4641.
PATRICi 23293933. VBIRhoPal84835_4873.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi AKEHREF.
OrthoDBi EOG66QKT8.
PhylomeDBi Q6N0W9.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01339. RuBisCO_L_type2.
InterProi IPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Construction of a genetically engineered microorganism for CO2 fixation using a Rhodopseudomonas/Escherichia coli shuttle vector."
    Du C., Zhou J., Wang J., Yan B., Lu H., Hou H.
    FEMS Microbiol. Lett. 225:69-73(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DH.
  2. "Analysis of diversity among 3-chlorobenzoate-degrading strains of Rhodopseudomonas palustris."
    Oda Y., Meijer W.G., Gibson J.L., Gottschal J.C., Forney L.J.
    Microb. Ecol. 47:68-79(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DCP3.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-98 / CGA009.

Entry informationi

Entry nameiRBL2_RHOPA
AccessioniPrimary (citable) accession number: Q6N0W9
Secondary accession number(s): Q8GJP8, Q93TJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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