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Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Albidiferax ferrireducens)
Status
Reviewed-Annotation score: 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.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

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111Substrate; in homodimeric partnerUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
Metal bindingi193 – 1931MagnesiumUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei321 – 3211SubstrateUniRule annotation
Sitei329 – 3291Transition state stabilizerUniRule annotation
Binding sitei368 – 3681SubstrateUniRule annotation

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

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciAFER338969:GHU9-1397-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:cbbMUniRule annotation
Ordered Locus Names:Rfer_1391
OrganismiRhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Albidiferax ferrireducens)
Taxonomic identifieri338969 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeRhodoferax
ProteomesiUP000008332 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Ribulose bisphosphate carboxylasePRO_0000251408Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi338969.Rfer_1391.

Structurei

3D structure databases

ProteinModelPortaliQ21YM9.
SMRiQ21YM9. Positions 2-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type II subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiNQYLHYH.
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.

Q21YM9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQSKRYADL SLQEAALIAG GQHILCAYKM APKDGLNYLE AAAHFAAESS
60 70 80 90 100
TGTNVEVCTT DDFTRDVDAL VYYVNEATED MRIAYPLALF DRNITDGRFM
110 120 130 140 150
LVSFLTLAVG NNQGMGDIKH AKMIDFYVPE RVIQMFDGPA KDISDLWRIL
160 170 180 190 200
GRPVKDGGFI VGTIIKPKLG LRPEPFAQAA YQFWLGGDFI KNDEPQGNQV
210 220 230 240 250
FSPIKKTLPL VYDALKRAQD ETGQAKLFSM NITADDHFEM CARADFALET
260 270 280 290 300
FGADADKLAF LVDGFVGGPG MVTTARRQYP NQYLHYHRGG HGMVTSPSSK
310 320 330 340 350
RGYTALVLAK MSRLQGASGI HVGTMGHGKM EGAGDDRVMA YMIERDECQG
360 370 380 390 400
PVYFQKWYGI KPTTPIVSGG MNALRLPGFF DNLGHGNIIN TAGGGSYGHL
410 420 430 440 450
DSPAAGAVSL RQAYECWKAG ADPIEWAKEH REFARAFESF PQDADRLFAG

WRDKLGVGA
Length:459
Mass (Da):50,391
Last modified:April 17, 2006 - v1
Checksum:i089F31E7B2FF938D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000267 Genomic DNA. Translation: ABD69124.1.
RefSeqiYP_522655.1. NC_007908.1.

Genome annotation databases

EnsemblBacteriaiABD69124; ABD69124; Rfer_1391.
KEGGirfr:Rfer_1391.
PATRICi23235349. VBIRhoFer131161_1696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000267 Genomic DNA. Translation: ABD69124.1.
RefSeqiYP_522655.1. NC_007908.1.

3D structure databases

ProteinModelPortaliQ21YM9.
SMRiQ21YM9. Positions 2-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338969.Rfer_1391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD69124; ABD69124; Rfer_1391.
KEGGirfr:Rfer_1391.
PATRICi23235349. VBIRhoFer131161_1696.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiNQYLHYH.
OrthoDBiEOG66QKT8.

Enzyme and pathway databases

BioCyciAFER338969:GHU9-1397-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.
    , Kyrpides N., Ivanova N., Richardson P.
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-621 / DSM 15236 / T118.

Entry informationi

Entry nameiRBL2_RHOFT
AccessioniPrimary (citable) accession number: Q21YM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2006
Last sequence update: April 17, 2006
Last modified: March 31, 2015
This is version 61 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.