ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q59637

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ODP1_PSEAE
Primary accession number Q59637
Secondary accession number Q9HUF3
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on January 11, 2001 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 60)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component
Synonym EC 1.2.4.1
Gene name
Name: aceE
Synonyms: aceA
OrderedLocusNames: PA5015
From
Pseudomonas aeruginosa [TaxID: 287] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=PAO;
PubMed=9171401 [NCBI, ExPASy, EBI, Israel, Japan]
Rae J.L., Cutfield J.F., Lamont I.L.;
"Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa.";
J. Bacteriol. 179:3561-3571(1997).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).
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: Homodimer (By similarity).
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
U47920; AAC45353.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG08400.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G83018; G83018.
RefSeq NP_253702.1; -.
3D structure databases
HSSP P06958; 1L8A. [HSSP ENTRY / PDB]
ModBase Q59637.
Enzyme and pathway databases
BioCyc PAER208964:PA5015-MON; -.
Organism-specific databases
PseudoCAP PA5015; -.
Family and domain databases
InterPro IPR004660; 2-oxoA_DHase_E1.
IPR005474; Transketo_N.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF00456; Transketolase_N; 2.
Pfam graphical view of domain structure.
PIRSF PIRSF000156; Pyruvate_dh_E1; 1.
TIGRFAMs TIGR00759; aceE; 1.
BLOCKS Q59637.
Genome annotation databases
GeneID 881326; -.
GenomeReviews AE004091_GR; PA5015.
KEGG pae:PA5015; -.
Phylogenomic databases
HOGENOM Q59637; -.
Genome annotation databases
CMR Q59637; PA5015.
Other
ProtoNet Q59637.
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   882  882     Pyruvate dehydrogenase E1 component. PRO_0000162247
CONFLICT   76    78        IRS -> DPLP (in Ref. 1; AAC45353). 
CONFLICT   149   156        EGRISEEQ -> GRPHQRRNK (in Ref. 1; AAC45353). 
CONFLICT   167   174        NGLSSYPH -> TACPPIRT (in Ref. 1; AAC45353). 
CONFLICT   377   377        Q -> H (in Ref. 1; AAC45353). 
CONFLICT   388   388        G -> V (in Ref. 1; AAC45353). 
CONFLICT   392   392        G -> A (in Ref. 1; AAC45353). 
CONFLICT   408   409        Missing (in Ref. 1). 
CONFLICT   517   517        A -> G (in Ref. 1; AAC45353). 
CONFLICT   671   671        Missing (in Ref. 1; AAC45353). 
CONFLICT   740   740        R -> H (in Ref. 1; AAC45353). 
CONFLICT   744   746        GIG -> DIV (in Ref. 1; AAC45353). 
CONFLICT   760   765        RDGLAV -> HDDLTL (in Ref. 1; AAC45353). 
CONFLICT   788   791        GRRG -> APSR (in Ref. 1; AAC45353). 
CONFLICT   821   821        Missing (in Ref. 1; AAC45353). 
Sequence information
Length: 882 AA [This is the length of the unprocessed precursor] Molecular weight: 99564 Da [This is the MW of the unprocessed precursor] CRC64: 5FD387B8332E24D9 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQDLDPVETQ EWLDALESVL DREGEDRAHY LMTRMGELAS RSGTQLPYAI TTPYRNTIPV 

        70         80         90        100        110        120 
THEARMPGDL FMERRIRSLV RWNALAMVMR ANKHDPDLGG HISTFASSAT LYDIGFNYFF 

       130        140        150        160        170        180 
QAPTDEHGGD LVFFQGHASP GVYARAFLEG RISEEQLENF RQEVDGNGLS SYPHPWLMPD 

       190        200        210        220        230        240 
FWQFPTVSMG LGPIQAIYQA RFMKYLESRG FIPAGKQKVW CFMGDGECDE PESLGAISLA 

       250        260        270        280        290        300 
GREKLDNLIF VINCNLQRLD GPVRGNAKII QELEGVFRGA EWNVNKVIWG RFWDPLFAKD 

       310        320        330        340        350        360 
TAGLLQQRMD EVIDGEYQNY KAKDGAYVRE HFFGARPELL EMVKDLSDEE IWKLNRGGHD 

       370        380        390        400        410        420 
PYKVYAAYHQ AVNHKGQPTV ILAKTIKGYG TGSGEAKNIA HNVKKVDVDS LRAFRDKFDI 

       430        440        450        460        470        480 
PVKDADLEKL PFYKPEEGSA EAKYLAERRA ALGGFMPVRR QKSMSVPVPP LETLKAMLDG 

       490        500        510        520        530        540 
SGDREISTTM AFVRIISQLV KDKELGPRIV PIVPDEARTF GMEGMFRQLG IYSSVGQLYE 

       550        560        570        580        590        600 
PVDKDQVMFY REDKKGQILE EGINEAGAMS SWIAAGTSYS THNQPMLPFY IFYSMFGFQR 

       610        620        630        640        650        660 
IGDLAWAAGD SRAHGFLIGG TAGRTTLNGE GLQHEDGHSH LLASTIPNCR TYDPTYAYEL 

       670        680        690        700        710        720 
AVIIREGSRQ MIEEQQDIFY YITVMNENYV QPAMPKGAEE GIIKGMYLLE EDKKEAAHHV 

       730        740        750        760        770        780 
QLLGSGTILR EVEEAAKLLR NDFGIGADVW SVPSFNELRR DGLAVERWNR LHPGQKPKQS 

       790        800        810        820        830        840 
YVEECLGGRR GPVIASTDYM KLYAEQIRQW VPSKEYKVLG TDGFGRSDSR KKLRNFFEVD 

       850        860        870        880 
RHWVVLAALE ALADRGDIEP KVVAEAIAKY GIDPEKRNPL DC
Q59637 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by kr flag YPRC Korea Mirror sites: Australia Brazil Canada China Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!