SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B3QB68

- RBL2_RHOPT

UniProt

B3QB68 - RBL2_RHOPT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase

Gene
cbbM, Rpal_5122
Organism
Rhodopseudomonas palustris (strain TIE-1)
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

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

Enzyme and pathway databases

BioCyciRPAL395960:GHPC-5175-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:cbbM
Ordered Locus Names:Rpal_5122
OrganismiRhodopseudomonas palustris (strain TIE-1)
Taxonomic identifieri395960 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001725: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Ribulose bisphosphate carboxylaseUniRule annotationPRO_1000142754Add
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

STRINGi395960.Rpal_5122.

Structurei

3D structure databases

ProteinModelPortaliB3QB68.
SMRiB3QB68. Positions 2-456.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiAKEHREF.
OrthoDBiEOG66QKT8.

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.

B3QB68-1 [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:September 2, 2008 - v1
Checksum:i907EFB041943AABC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001096 Genomic DNA. Translation: ACF03611.1.
RefSeqiYP_001994086.1. NC_011004.1.

Genome annotation databases

EnsemblBacteriaiACF03611; ACF03611; Rpal_5122.
GeneIDi6412816.
KEGGirpt:Rpal_5122.
PATRICi23314835. VBIRhoPal88240_5197.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001096 Genomic DNA. Translation: ACF03611.1 .
RefSeqi YP_001994086.1. NC_011004.1.

3D structure databases

ProteinModelPortali B3QB68.
SMRi B3QB68. Positions 2-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 395960.Rpal_5122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF03611 ; ACF03611 ; Rpal_5122 .
GeneIDi 6412816.
KEGGi rpt:Rpal_5122.
PATRICi 23314835. VBIRhoPal88240_5197.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RPAL395960:GHPC-5175-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TIE-1.

Entry informationi

Entry nameiRBL2_RHOPT
AccessioniPrimary (citable) accession number: B3QB68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: May 14, 2014
This is version 37 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

Similar proteinsi