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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

Dlat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.By similarity

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei615Sequence analysis1
Active sitei619Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-5362517. Signaling by Retinoic Acid.
R-MMU-70268. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name:
PDC-E2
Short name:
PDCE2
Gene namesi
Name:Dlat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2385311. Dlat.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial pyruvate dehydrogenase complex Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • pyruvate dehydrogenase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 85MitochondrionBy similarityAdd BLAST85
ChainiPRO_000028571786 – 642Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialAdd BLAST557

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei99PhosphoserineBy similarity1
Modified residuei131N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei258N6-lipoyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei461N6-acetyllysineBy similarity1
Modified residuei468N6-succinyllysineCombined sources1
Modified residuei542N6-succinyllysineCombined sources1

Post-translational modificationi

Delipoylated at Lys-131 and Lys-258 by SIRT4, delipoylation decreases the PHD complex activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BMF4.
MaxQBiQ8BMF4.
PaxDbiQ8BMF4.
PeptideAtlasiQ8BMF4.
PRIDEiQ8BMF4.

2D gel databases

REPRODUCTION-2DPAGEIPI00153660.
UCD-2DPAGEQ8BMF4.

PTM databases

iPTMnetiQ8BMF4.
PhosphoSitePlusiQ8BMF4.
SwissPalmiQ8BMF4.

Expressioni

Gene expression databases

BgeeiENSMUSG00000000168.
GenevisibleiQ8BMF4. MM.

Interactioni

Subunit structurei

Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3. Interacts with SIRT4 (By similarity).By similarity

Protein-protein interaction databases

BioGridi231646. 3 interactors.
IntActiQ8BMF4. 7 interactors.
MINTiMINT-135876.
STRINGi10090.ENSMUSP00000034567.

Structurei

3D structure databases

ProteinModelPortaliQ8BMF4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini90 – 166Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST77
Domaini217 – 293Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni353 – 384E3- and/or E1-component binding domainSequence analysisAdd BLAST32
Regioni466 – 642CatalyticBy similarityAdd BLAST177
Regioni610 – 621CoA-bindingBy similarityAdd BLAST12

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG0557. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133743.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiQ8BMF4.
KOiK00627.
OMAiVESCIIT.
OrthoDBiEOG091G0CAV.
PhylomeDBiQ8BMF4.
TreeFamiTF106145.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
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.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BMF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRVCARRAR SAVPRDGFRA RWAALKEGPG APCGSPRIGP AAVRCGSGIP
60 70 80 90 100
RYGVRSLCGW SSGSGTVPRN RLLRQLLGSP SRRSYSLPPH QKVPLPSLSP
110 120 130 140 150
TMQAGTIARW EKKEGEKISE GDLIAEVETD KATVGFESLE ECYMAKILVP
160 170 180 190 200
EGTRDVPVGS IICITVEKPQ DIEAFKNYTL DLAAAAAPQA APAAAPAPAA
210 220 230 240 250
APAAPSASAP GSSYPTHMQI VLPALSPTMT MGTVQRWEKK VGEKLSEGDL
260 270 280 290 300
LAEIETDKAT IGFEVQEEGY LAKILVPEGT RDVPLGAPLC IIVEKQEDIA
310 320 330 340 350
AFADYRPTEV TSLKPQAAPP APPPVAAVPP TPQPVAPTPS AAPAGPKGRV
360 370 380 390 400
FVSPLAKKLA AEKGIDLTQV KGTGPEGRII KKDIDSFVPS KAAPAAAAAM
410 420 430 440 450
APPGPRVAPA PAGVFTDIPI SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG
460 470 480 490 500
EVLLVRKELN KMLEGKGKIS VNDFIIKASA LACLKVPEAN SSWMDTVIRQ
510 520 530 540 550
NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA SKAREGKLQP
560 570 580 590 600
HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG
610 620 630 640
FDVASVMSVT LSCDHRVVDG AVGAQWLAEF KKYLEKPITM LL
Length:642
Mass (Da):67,942
Last modified:May 1, 2007 - v2
Checksum:i1294FAC4857FC29C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84S → Y in AAL02400 (PubMed:12108679).Curated1
Sequence conflicti198P → T in BAC27715 (PubMed:16141072).Curated1
Sequence conflicti225L → P in AAL02400 (PubMed:12108679).Curated1
Sequence conflicti393A → V in AAH31495 (PubMed:15489334).Curated1
Sequence conflicti604A → V in AAH31495 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK032124 mRNA. Translation: BAC27715.1.
BC026680 mRNA. Translation: AAH26680.1.
BC031495 mRNA. Translation: AAH31495.1.
BC069862 mRNA. Translation: AAH69862.1.
AY044265 mRNA. Translation: AAL02400.1.
CCDSiCCDS23168.1.
RefSeqiNP_663589.3. NM_145614.4.
UniGeneiMm.285076.
Mm.471144.

Genome annotation databases

EnsembliENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168.
GeneIDi235339.
KEGGimmu:235339.
UCSCiuc009pka.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK032124 mRNA. Translation: BAC27715.1.
BC026680 mRNA. Translation: AAH26680.1.
BC031495 mRNA. Translation: AAH31495.1.
BC069862 mRNA. Translation: AAH69862.1.
AY044265 mRNA. Translation: AAL02400.1.
CCDSiCCDS23168.1.
RefSeqiNP_663589.3. NM_145614.4.
UniGeneiMm.285076.
Mm.471144.

3D structure databases

ProteinModelPortaliQ8BMF4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231646. 3 interactors.
IntActiQ8BMF4. 7 interactors.
MINTiMINT-135876.
STRINGi10090.ENSMUSP00000034567.

PTM databases

iPTMnetiQ8BMF4.
PhosphoSitePlusiQ8BMF4.
SwissPalmiQ8BMF4.

2D gel databases

REPRODUCTION-2DPAGEIPI00153660.
UCD-2DPAGEQ8BMF4.

Proteomic databases

EPDiQ8BMF4.
MaxQBiQ8BMF4.
PaxDbiQ8BMF4.
PeptideAtlasiQ8BMF4.
PRIDEiQ8BMF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168.
GeneIDi235339.
KEGGimmu:235339.
UCSCiuc009pka.2. mouse.

Organism-specific databases

CTDi1737.
MGIiMGI:2385311. Dlat.

Phylogenomic databases

eggNOGiKOG0557. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133743.
HOGENOMiHOG000281566.
HOVERGENiHBG005063.
InParanoidiQ8BMF4.
KOiK00627.
OMAiVESCIIT.
OrthoDBiEOG091G0CAV.
PhylomeDBiQ8BMF4.
TreeFamiTF106145.

Enzyme and pathway databases

ReactomeiR-MMU-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-5362517. Signaling by Retinoic Acid.
R-MMU-70268. Pyruvate metabolism.

Miscellaneous databases

ChiTaRSiDlat. mouse.
PROiQ8BMF4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000168.
GenevisibleiQ8BMF4. MM.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
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.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODP2_MOUSE
AccessioniPrimary (citable) accession number: Q8BMF4
Secondary accession number(s): Q8K2G8, Q8R339, Q91ZB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: November 30, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.