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Q59638

- ODP2_PSEAE

UniProt

Q59638 - ODP2_PSEAE

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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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).

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

Binds 2 lipoyl cofactors covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei520 – 5201Sequence Analysis

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
Gene namesi
Name:aceF
Synonyms:aceB
Ordered Locus Names:PA5016
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA5016.

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-lipoyllysineBy similarity
Modified residuei159 – 1591N6-lipoyllysineBy similarity

2D gel databases

World-2DPAGE0008:Q59638.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

STRINGi208964.PA5016.

Structurei

3D structure databases

ProteinModelPortaliQ59638.
SMRiQ59638. Positions 2-81, 119-198, 246-285, 305-547.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7474Lipoyl-binding 1Add
BLAST
Domaini120 – 19273Lipoyl-binding 2Add
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 2 lipoyl-binding domains.Curated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
InParanoidiQ59638.
KOiK00627.
OMAiTEIMVAV.
PhylomeDBiQ59638.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59638-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSELIRVPDI GNGEGEVIEL LVKPGDKVEA DQSLLTLESD KASMEIPSPK
60 70 80 90 100
AGVVKSIKAK VGDTLKEGDE ILELEVEGGE QPAEAKAEAA PAQPEAPKAE
110 120 130 140 150
APAPAPSESK PAAPAAASVQ DIKVPDIGSA GKANVIEVMV KAGDTVEADQ
160 170 180 190 200
SLITLESDKA SMEIPSPASG VVESVSIKVG DEVGTGDLIL KLKVEGAAPA
210 220 230 240 250
AEEQPAAAPA QAAAPAAEQK PAAAAPAPAK ADTPAPVGAP SRDGAKVHAG
260 270 280 290 300
PAVRMLAREF GVELSEVKAS GPKGRILKED VQVFVKEQLQ RAKSGGAGAT
310 320 330 340 350
GGAGIPPIPE VDFSKFGEVE EVAMTRLMQV GAANLHRSWL NVPHVTQFDQ
360 370 380 390 400
SDITDMEAFR VAQKAAAEKA GVKLTVLPIL LKACAHLLKE LPDFNSSLAP
410 420 430 440 450
SGKALIRKKY VHIGFAVDTP DGLLVPVIRD VDRKSLLQLA AEAADLADKA
460 470 480 490 500
RNKKLSADAM QGACFTISSL GHIGGTGFTP IVNAPEVAIL GVSKATMQPV
510 520 530 540
WDGKAFQPRL MLPLSLSYDH RVINGAAAAR FTKRLGELLA DIRTLLL
Length:547
Mass (Da):56,709
Last modified:December 8, 2000 - v2
Checksum:i24E15CCC9A590CB4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251A → V in AAC45354. (PubMed:9171401)Curated
Sequence conflicti295 – 3017GGAGATG → AVPAPR in AAC45354. (PubMed:9171401)Curated
Sequence conflicti328 – 3292MQ → IE in AAC45354. (PubMed:9171401)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U47920 Genomic DNA. Translation: AAC45354.1.
AE004091 Genomic DNA. Translation: AAG08401.1.
PIRiH83018.
RefSeqiNP_253703.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG08401; AAG08401; PA5016.
GeneIDi881297.
KEGGipae:PA5016.
PATRICi19844857. VBIPseAer58763_5257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U47920 Genomic DNA. Translation: AAC45354.1 .
AE004091 Genomic DNA. Translation: AAG08401.1 .
PIRi H83018.
RefSeqi NP_253703.1. NC_002516.2.

3D structure databases

ProteinModelPortali Q59638.
SMRi Q59638. Positions 2-81, 119-198, 246-285, 305-547.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA5016.

2D gel databases

World-2DPAGE 0008:Q59638.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG08401 ; AAG08401 ; PA5016 .
GeneIDi 881297.
KEGGi pae:PA5016.
PATRICi 19844857. VBIPseAer58763_5257.

Organism-specific databases

PseudoCAPi PA5016.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281562.
InParanoidi Q59638.
KOi K00627.
OMAi TEIMVAV.
PhylomeDBi Q59638.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: PAO.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiODP2_PSEAE
AccessioniPrimary (citable) accession number: Q59638
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: October 29, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3