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O66112 (ODPA_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

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

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit alpha

EC=1.2.4.1
Gene names
Name:pdhA
Synonyms:pdhAalpha
Ordered Locus Names:ZMO1606
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length354 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

Thiamine pyrophosphate By similarity.

Subunit structure

Heterodimer of an alpha and a beta chain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintracellular membrane-bounded organelle

Inferred from electronic annotation. Source: InterPro

   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 – 354354Pyruvate dehydrogenase E1 component subunit alpha
PRO_0000162213

Experimental info

Sequence conflict691C → N in AAC70361. Ref.2
Sequence conflict3091Missing in AAC70361. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O66112 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 515F5B2EDA0C1424

FASTA35438,654
        10         20         30         40         50         60 
MAKATQDSNR PHKADVGSAI PNHDLPPIPG RYHADREELL EFYRRMLMIR RFEERCGQLY 

        70         80         90        100        110        120 
GLGLIAGFCH LYIGQEAVAV GLQAALQPGR DSVITGYREH GHMLAYGIDP KIVMAELTGR 

       130        140        150        160        170        180 
ASGISHGKGG SMHMFSTEHK FFGGNGIVGA QVPLGAGLAF AHKYRNDGGC SAAYFGDGSA 

       190        200        210        220        230        240 
NQGQVYEAYN MAALWKLPVI FVIENNGYAM GTSIQRANAH TALSERGAGF GIPALVVDGM 

       250        260        270        280        290        300 
DVLEVRGAAT VAVDWVQAGK GPIILEMKTY RYRGHSMSDP ARYRSREEVN DMKENHDPLD 

       310        320        330        340        350 
NLKKDLFAAG VPEAELVKLD EDIRQQVKEA ADFAEKAPLP ADEELYTNIL VGKY 

« 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: CAA73384.1.
AF086791 Genomic DNA. Translation: AAC70361.1.
AE008692 Genomic DNA. Translation: AAV90230.1.
PIRT33722.
RefSeqYP_163341.1. NC_006526.2.

3D structure databases

ProteinModelPortalO66112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264203.ZMO1606.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV90230; AAV90230; ZMO1606.
GeneID3187783.
KEGGzmo:ZMO1606.
PATRIC32568470. VBIZymMob102260_1511.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281336.
KOK00161.
OMAEYAMGTS.
OrthoDBEOG6JMMWC.

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-1992-MONOMER.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_ZYMMO
AccessionPrimary (citable) accession number: O66112
Secondary accession number(s): O69011, Q5NM30
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program