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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

Dlat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processCarbohydrate 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2385311 Dlat

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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-2DPAGEiIPI00153660
UCD-2DPAGEiQ8BMF4

PTM databases

iPTMnetiQ8BMF4
PhosphoSitePlusiQ8BMF4
SwissPalmiQ8BMF4

Expressioni

Gene expression databases

BgeeiENSMUSG00000000168 Expressed in 297 organ(s), highest expression level in brown adipose tissue
GenevisibleiQ8BMF4 MM

Interactioni

Subunit structurei

Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, 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. Interacts with PDHB.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi231646, 4 interactors
IntActiQ8BMF4, 10 interactors
MINTiQ8BMF4
STRINGi10090.ENSMUSP00000034567

Structurei

3D structure databases

ProteinModelPortaliQ8BMF4
SMRiQ8BMF4
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
Domaini351 – 388Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni466 – 642CatalyticBy similarityAdd BLAST177
Regioni610 – 621CoA-bindingBy similarityAdd BLAST12

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG0557 Eukaryota
COG0508 LUCA
GeneTreeiENSGT00890000139393
HOGENOMiHOG000281566
HOVERGENiHBG005063
InParanoidiQ8BMF4
KOiK00627
OMAiTMEFESF
OrthoDBiEOG091G0CAV
PhylomeDBiQ8BMF4
TreeFamiTF106145

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 2 hits
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 2 hits
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 2 hits
PS00189 LIPOYL, 2 hits
PS51826 PSBD, 1 hit

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

Similar proteinsi

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
SMRiQ8BMF4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231646, 4 interactors
IntActiQ8BMF4, 10 interactors
MINTiQ8BMF4
STRINGi10090.ENSMUSP00000034567

PTM databases

iPTMnetiQ8BMF4
PhosphoSitePlusiQ8BMF4
SwissPalmiQ8BMF4

2D gel databases

REPRODUCTION-2DPAGEiIPI00153660
UCD-2DPAGEiQ8BMF4

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
GeneTreeiENSGT00890000139393
HOGENOMiHOG000281566
HOVERGENiHBG005063
InParanoidiQ8BMF4
KOiK00627
OMAiTMEFESF
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
PROiPR:Q8BMF4
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000168 Expressed in 297 organ(s), highest expression level in brown adipose tissue
GenevisibleiQ8BMF4 MM

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 2 hits
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 2 hits
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 2 hits
PS00189 LIPOYL, 2 hits
PS51826 PSBD, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiODP2_MOUSE
AccessioniPrimary (citable) accession number: Q8BMF4
Secondary accession number(s): Q8K2G8, Q8R339, Q91ZB1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: September 12, 2018
This is version 132 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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