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O66113 (ODPB_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:ZMO1605
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas ›

Protein attributes

Sequence length462 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.

Binds 1 thiamine pyrophosphate per subunit.

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_processacetyl-CoA biosynthetic process from pyruvate

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162237

Regions

Domain1 – 7777Lipoyl-binding

Sites

Binding site1951Thiamine pyrophosphate By similarity

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Experimental info

Sequence conflict871D → E in CAA73385. Ref.1
Sequence conflict1121V → L in CAA73385. Ref.1
Sequence conflict232 – 24413SAAKT…SGGQV → LRPKRIICPAAKC Ref.2
Sequence conflict2591R → P in AAC70362. Ref.2
Sequence conflict2621A → E in AAC70362. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O66113 [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: 00F53CE4A5731F1C

FASTA46249,833
        10         20         30         40         50         60 
MAIELKMPAL SPTMEEGTLT RWLVKEGDSI KAGEILAEIE TDKAIMEFEA VDEGVITKIL 

        70         80         90        100        110        120 
IPEGSENVKV GTAIAYLGTD ANDVTLDGAS AETKAEESAP VASPAKTEAA AVEEAATPSL 

       130        140        150        160        170        180 
GKVINSAPEI PEGTEFFQQT LREALRDAMA EEMRRDDRVF VMGEEVAEYQ GAYKVTQGLL 

       190        200        210        220        230        240 
QEFGARRVVD TPISEYGFSG IGVGAAMEGL RPVIEFMTMN FSMQAIDHII NSAAKTHYMS 

       250        260        270        280        290        300 
GGQVRCPIVF RGPNGAAPRV GAQHTQNFGP WYAAVPGLVV LAPYDAIDAK GLLKAAIRSD 

       310        320        330        340        350        360 
DPVVFLECEL LYGKTFDVPK MDDFVLPIGK ARIIREGKDV TIVSYSIGVS FALTAAEALA 

       370        380        390        400        410        420 
KEGIDAEVID LRTLRPLDKE TILQSLAKTN RIVTVEDGWP VCSISSEIAA IAMEEGFDNL 

       430        440        450        460 
DAPVLRVTNA DTPTPYAENL EKKGLVNPEA IIEAVRKVCY RK

« Hide

References

« Hide 'large scale' references
[1]"Purification of the pyruvate dehydrogenase multienzyme complex of Zymomonas mobilis and identification and sequence analysis of the corresponding genes."
Neveling U., Klasen R., Bringer-Meyer S., Sahm H.
J. Bacteriol. 180:1540-1548(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[2]Lee J., Jin S., Kang H.S.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.
[3]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y12884 Genomic DNA. Translation: CAA73385.1.
AF086791 Genomic DNA. Translation: AAC70362.1.
AE008692 Genomic DNA. Translation: AAV90229.1.
PIRT33723.
RefSeqYP_163340.1. NC_006526.2.

3D structure databases

ProteinModelPortalO66113.
SMRO66113. Positions 138-459.
ModBaseSearch...

Protein-protein interaction databases

STRING264203.ZMO1605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV90229; AAV90229; ZMO1605.
GeneID3187757.
KEGGzmo:ZMO1605.
PATRIC32568468. VBIZymMob102260_1510.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281450.
KOK00162.
OMAQHSQDYS.
ProtClustDBPRK11892.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR027110. PDHB.
IPR011053. Single_hybrid_motif.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERPTHR11624:SF11. PTHR11624:SF11. 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. Hybrid_motif. 1 hit.
SSF52922. Transketo_C_like. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODPB_ZYMMO
AccessionPrimary (citable) accession number: O66113
Secondary accession number(s): O69012, Q5NM31
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: May 1, 2013
This is version 95 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

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