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Q9R9N4 (ODPB_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit beta

EC=1.2.4.1
Gene names
Name:pdhB
Synonyms:pdhAbeta
Ordered Locus Names:R01446
ORF Names:SMc01031
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Binds 1 thiamine pyrophosphate per subunit By similarity.

Subunit structure

Heterodimer of an alpha and a beta chain.

Sequence similarities

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162225

Regions

Domain1 – 7777Lipoyl-binding

Sites

Binding site1941Thiamine pyrophosphate By similarity

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Experimental info

Sequence conflict531E → K in AAF04588. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R9N4 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 9FA3E5A30EDC3C6F

FASTA46048,812
        10         20         30         40         50         60 
MPVEILMPAL SPTMEEGTLS KWLKNEGDKV SSGDVIAEIE TDKATMEVEA VDEGTIGKLL 

        70         80         90        100        110        120 
IAAGTEGVKV NTPIAVLLQD GEAASDIDSM KTEAPKAETP KPAAAEAPAA SAAPVAAQPK 

       130        140        150        160        170        180 
ADVPSDPAIP AGTEMATMTV REALRDAMAE EMRANEDVFV MGEEVAEYQG AYKVTQGLLQ 

       190        200        210        220        230        240 
EFGARRVVDT PITEHGFAGV GVGAAMTGLR PIVEFMTFNF AMQAIDQIIN SAAKTLYMSG 

       250        260        270        280        290        300 
GQMGAPIVFR GPSGAAARVA AQHSQCYAAW YSHIPGLKVV MPYTAADAKG LLKAAIRDPN 

       310        320        330        340        350        360 
PVIFLENEIL YGQSFEVPKL DDFVLPIGKA RIHRTGKDAT LVSFGIGMTY AIKAAAELEA 

       370        380        390        400        410        420 
QGIDVEIIDL RTIRPMDLPT VIESVKKTGR LVTVEEGYPQ SSVGTEIATR VMQQAFDYLD 

       430        440        450        460 
APILTIAGKD VPMPYAANLE KLALPNVAEV VDAVKAVCYK 

« Hide

References

« Hide 'large scale' references
[1]"Symbiotic induction of pyruvate dehydrogenase genes from Sinorhizobium meliloti."
Cabanes D., Boistard P., Batut J.
Mol. Plant Microbe Interact. 13:483-493(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RCR2011 / SU47.
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF190792 Genomic DNA. Translation: AAF04588.1.
AL591688 Genomic DNA. Translation: CAC46025.1.
RefSeqNP_385552.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ9R9N4.
SMRQ9R9N4. Positions 137-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc01031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC46025; CAC46025; SMc01031.
GeneID1233099.
KEGGsme:SMc01031.
PATRIC23632229. VBISinMel96828_2866.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281450.
KOK00162.
OMAEISTHSF.
OrthoDBEOG6JQH4C.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-1481-MONOMER.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR027110. PDHB.
IPR011053. Single_hybrid_motif.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamPF00364. Biotin_lipoyl. 1 hit.
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODPB_RHIME
AccessionPrimary (citable) accession number: Q9R9N4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: June 11, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families