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Reviewed, UniProtKB/Swiss-Prot O66112 (ODPA_ZYMMO)

Last modified November 3, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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 [Complete proteome] [HAMAP]
Taxonomic identifier542 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

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: 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
O66112-1 [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: 9515924] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29191 / DSM 3580 / IFO 13756 / NCIB 11199 / 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: 15592456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

Y12884 Genomic DNA. Translation: CAA73384.1.
AF086791 Genomic DNA. Translation: AAC70361.1.
AE008692 Genomic DNA. Translation: AAV90230.1.
PIRT33722.
RefSeqYP_163341.1.

3D structure databases

HSSPHSSP built from PDB template 1NI4 based on UniProtKB P08559.
ModBaseSearch...

Genome annotation databases

GeneID3187783.
GenomeReviewsGene locus ZMO1606 in contig AE008692_GR.
KEGGzmo:ZMO1606.
NMPDRfig|264203.3.peg.80.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO66112.
OMALEYETYR.

Enzyme and pathway databases

BioCycZMOB264203:ZMO1606-MON.
BRENDA1.2.4.1. 1658.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
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: November 3, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information