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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • (R)-lipoateUniRule annotationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 2 lipoyl cofactors covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 3 lipoyl cofactors covalently.UniRule annotation

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: JCVI

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: JCVI
  2. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

PyruvateImported

Enzyme and pathway databases

BioCyciPFLU220664:GIX8-509-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Name:aceFImported
Ordered Locus Names:PFL_0508Imported
OrganismiPseudomonas fluorescens (strain Pf-5 / ATCC BAA-477)Imported
Taxonomic identifieri220664 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000008540 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.UniRule annotation

Protein-protein interaction databases

STRINGi220664.PFL_0508.

Structurei

3D structure databases

ProteinModelPortaliQ4KJD1.
SMRiQ4KJD1. Positions 2-80, 407-649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 3 lipoyl-binding domains.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.

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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4KJD1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELIRVPDI GSGEGEVIEL FVKVGDRIEA DQSILTLESD KASMEVPAPK
60 70 80 90 100
AGVIKSLKVK LGDRLKEGDE LLELEVEGAA AAAPAAAPAA KAEAKPAAAP
110 120 130 140 150
AAASAPAAAP AAASVQQVHV PDIGSSGKAQ IIEIQVKVGD KVEADQSLIT
160 170 180 190 200
LESDKASMEI PSPAAGVVKA ISVKLNDEVG TGDLILDLEV AGAAAPAAAP
210 220 230 240 250
AQAAAPAAAA APAPAAAPAA PVADSVQDIH VPDIGSAGKA KIIEVLVKAG
260 270 280 290 300
DSVEADQSLI TLESDKASME IPSPAAGVVE SVSIKLDDEV GTGDLILKLK
310 320 330 340 350
VKGAAPAAAP APAAAPSAPA PAAAAAPAAA APAAAPAAAP AKPGAKVHAG
360 370 380 390 400
PAVRQLAREF GVELSAVGAS GPHGRILKED VQVYVKAMMQ KAKEAPAAGG
410 420 430 440 450
ATGGAGIPPI PVVDFSRFGE IEEVPMTRLM QAGAANLHRS WLNVPHVTQF
460 470 480 490 500
DSADITELEA FRVAQKAVAE KAGVKLTILP LLLKSCAHLL KELPDFNSSL
510 520 530 540 550
APSGKAIIRK KYVNIGFAVD TPDGLLVPVI KNVDQKSLLQ LAAEAASLAE
560 570 580 590 600
KARTKKLSAD EMQGACFTIS SLGHIGGTGF TPIVNAPEVA ILGVSKATIQ
610 620 630 640
PVWDGKAFQP KLMLPLSLSY DHRVINGAAA ARFTKRLSDL LADIRTILL
Length:649
Mass (Da):65,685
Last modified:August 1, 2005 - v1
Checksum:i8089F14059C1D2BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000076 Genomic DNA. Translation: AAY95917.1.
RefSeqiYP_257652.1. NC_004129.6.

Genome annotation databases

EnsemblBacteriaiAAY95917; AAY95917; PFL_0508.
KEGGipfl:PFL_0508.
PATRICi19870169. VBIPseFlu72549_0523.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000076 Genomic DNA. Translation: AAY95917.1.
RefSeqiYP_257652.1. NC_004129.6.

3D structure databases

ProteinModelPortaliQ4KJD1.
SMRiQ4KJD1. Positions 2-80, 407-649.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi220664.PFL_0508.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAY95917; AAY95917; PFL_0508.
KEGGipfl:PFL_0508.
PATRICi19870169. VBIPseFlu72549_0523.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.

Enzyme and pathway databases

BioCyciPFLU220664:GIX8-509-MONOMER.

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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pf-5 / ATCC BAA-477Imported.

Entry informationi

Entry nameiQ4KJD1_PSEF5
AccessioniPrimary (citable) accession number: Q4KJD1
Entry historyi
Integrated into UniProtKB/TrEMBL: August 1, 2005
Last sequence update: August 1, 2005
Last modified: March 31, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.