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UniProtKB/Swiss-Prot entry O66112


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPA_ZYMMO
Primary accession number O66112
Secondary accession numbers O69011 Q5NM30
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 51)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha
Synonym EC 1.2.4.1
Gene name
Name: pdhA
Synonyms: pdhAalpha
OrderedLocusNames: ZMO1606
From
Zymomonas mobilis [TaxID: 542] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Zymomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 29191 / DSM 3580 / IFO 13756 / NCIB 11199 / ZM6;
PubMed=9515924 [NCBI, ExPASy, EBI, Israel, Japan]
Neveling U., Klasen R., Bringer-Meyer S., Sahm H.;
"Purification of the pyruvate dehydrogenase multienzyme complex of Zymomonas mobilis and identification and sequence analysis of the corresponding genes.";
J. Bacteriol. 180:1540-1548(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 31821 / ZM4 / CP4;
Lee J., Jin S., Kang H.S.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 31821 / ZM4 / CP4;
DOI=10.1038/nbt1045; PubMed=15592456 [NCBI, ExPASy, EBI, Israel, Japan]
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., Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4.";
Nat. Biotechnol. 23:63-68(2005).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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: Heterodimer of an alpha and a beta chain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y12884; CAA73384.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF086791; AAC70361.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008692; AAV90230.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T33722; T33722.
RefSeq YP_163341.1; -.
3D structure databases
HSSP P08559; 1NI4. [HSSP ENTRY / PDB]
ModBase O66112.
Enzyme and pathway databases
BioCyc ZMOB264203:ZMO1606-MON; -.
Ontologies
GO
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
Genome annotation databases
GeneID 3187783; -.
GenomeReviews AE008692_GR; ZMO1606.
KEGG zmo:ZMO1606; -.
NMPDR fig|264203.3.peg.80; -.
Phylogenomic databases
HOGENOM O66112; -.
Genome annotation databases
CMR O66112; ZMO1606.
Other
ProtoNet O66112.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   354  354     Pyruvate dehydrogenase E1 component subunit alpha. PRO_0000162213
CONFLICT   69    69        C -> N (in Ref. 2; AAC70361). 
CONFLICT   309   309        Missing (in Ref. 2; AAC70361). 
Sequence information
Length: 354 AA [This is the length of the unprocessed precursor] Molecular weight: 38654 Da [This is the MW of the unprocessed precursor] CRC64: 515F5B2EDA0C1424 [This is a checksum on the sequence]
        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 

O66112 in FASTA format

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