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Reviewed, UniProtKB/Swiss-Prot Q59637 (ODP1_PSEAE)

Last modified November 4, 2008. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 · Relevant documents

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Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component
    EC=1.2.4.1
Gene names
Name: aceE
Synonyms: aceA
Ordered Locus Names: PA5015
OrganismPseudomonas aeruginosa [Complete proteome] [HAMAP]
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length882 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (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 + CO(2).

Cofactor

Thiamine pyrophosphate By similarity.

Subunit structure

Homodimer By similarity.

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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

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 882882Pyruvate dehydrogenase E1 component
PRO_0000162247

Experimental info

Sequence conflict76 – 783IRS → DPLP in AAC45353. Ref.1
Sequence conflict149 – 1568EGRISEEQ → GRPHQRRNK in AAC45353. Ref.1
Sequence conflict167 – 1748NGLSSYPH → TACPPIRT in AAC45353. Ref.1
Sequence conflict3771Q → H in AAC45353. Ref.1
Sequence conflict3881G → V in AAC45353. Ref.1
Sequence conflict3921G → A in AAC45353. Ref.1
Sequence conflict408 – 4092Missing Ref.1
Sequence conflict5171A → G in AAC45353. Ref.1
Sequence conflict6711Missing in AAC45353. Ref.1
Sequence conflict7401R → H in AAC45353. Ref.1
Sequence conflict744 – 7463GIG → DIV in AAC45353. Ref.1
Sequence conflict760 – 7656RDGLAV → HDDLTL in AAC45353. Ref.1
Sequence conflict788 – 7914GRRG → APSR in AAC45353. Ref.1
Sequence conflict8211Missing in AAC45353. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q59637-1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 5FD387B8332E24D9

FASTA88299,564
        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

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References

« Hide 'large scale' references
[1]"Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa."
Rae J.L., Cutfield J.F., Lamont I.L.
J. Bacteriol. 179:3561-3571(1997) [PubMed: 9171401] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PAO.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
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. expand/collapse author list , 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.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

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Cross-references

Sequence databases

U47920 Genomic DNA. Translation: AAC45353.1.
AE004091 Genomic DNA. Translation: AAG08400.1.
PIRG83018.
RefSeqNP_253702.1.

3D structure databases

HSSPHSSP built from PDB template 1L8A based on UniProtKB P06958.
ModBaseSearch...

Genome annotation databases

GeneID881326.
GenomeReviewsGene locus PA5015 in contig AE004091_GR.
KEGGpae:PA5015.

Organism-specific databases

PseudoCAPPA5015.
CMRSearch...

Phylogenomic databases

HOGENOMQ59637.

Enzyme and pathway databases

BioCycPAER208964:PA5015-MON.

Family and domain databases

InterProIPR004660. 2-oxoA_DHase_E1.
IPR005474. Transketo_N.
IPR015941. Transketolase_C-like.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF00456. Transketolase_N. 2 hits.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
TIGRFAMsTIGR00759. aceE. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameODP1_PSEAE
AccessionPrimary (citable) accession number: Q59637
Secondary accession number(s): Q9HUF3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: November 4, 2008
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents