Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial

Gene

Dbt

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

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component.

Catalytic activityi

2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei452Sequence analysis1
Active sitei456Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-70895. Branched-chain amino acid catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC:2.3.1.168)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase complex component E2
Short name:
BCKAD-E2
Short name:
BCKADE2
Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
Dihydrolipoamide branched chain transacylase
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase
Gene namesi
Name:Dbt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:105386. Dbt.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial nucleoid Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 61MitochondrionSequence analysisAdd BLAST61
ChainiPRO_000002049062 – 482Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialAdd BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei105N6-lipoyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei133N6-succinyllysineCombined sources1
Modified residuei196N6-acetyllysine; alternateCombined sources1
Modified residuei196N6-succinyllysine; alternateCombined sources1
Modified residuei202N6-acetyllysineCombined sources1
Modified residuei220PhosphoserineBy similarity1
Modified residuei243N6-acetyllysineCombined sources1
Modified residuei250N6-acetyllysineCombined sources1
Modified residuei261N6-succinyllysineCombined sources1
Modified residuei289N6-acetyllysine; alternateCombined sources1
Modified residuei289N6-succinyllysine; alternateCombined sources1
Modified residuei295N6-acetyllysineCombined sources1
Modified residuei304N6-acetyllysineCombined sources1
Modified residuei435N6-acetyllysineCombined sources1
Modified residuei440N6-acetyllysine; alternateCombined sources1
Modified residuei440N6-succinyllysine; alternateCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP53395.
MaxQBiP53395.
PaxDbiP53395.
PeptideAtlasiP53395.
PRIDEiP53395.

PTM databases

iPTMnetiP53395.
PhosphoSitePlusiP53395.
SwissPalmiP53395.

Expressioni

Gene expression databases

BgeeiENSMUSG00000000340.
CleanExiMM_DBT.
ExpressionAtlasiP53395. baseline and differential.
GenevisibleiP53395. MM.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199061. 6 interactors.
IntActiP53395. 5 interactors.
MINTiMINT-1860345.
STRINGi10090.ENSMUSP00000000349.

Structurei

3D structure databases

ProteinModelPortaliP53395.
SMRiP53395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 139Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0558. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133743.
HOGENOMiHOG000281564.
HOVERGENiHBG104085.
InParanoidiP53395.
KOiK09699.
OMAiTIPHFTY.
OrthoDBiEOG091G0FJ3.
TreeFamiTF314182.

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.
IPR015761. BCKDC_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR23151:SF71. PTHR23151:SF71. 2 hits.
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P53395-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAARVLRTW SQNAVRLTCV RYFQTFNSAR VLKPKCVCSV GYPLFKYSQP
60 70 80 90 100
RHSLRTAAVL QGQVVQFKLS DIGEGIREVT IKEWYVKEGD TVSQFDSICE
110 120 130 140 150
VQSDKASVTI TSRYDGVIKR LYYNLDDIAY VGKPLIDIET EALKDSEEDV
160 170 180 190 200
VETPAVSHDE HTHQEIKGQK TLATPAVRRL AMENNIKLSE VVGSGKDGRI
210 220 230 240 250
LKEDILSFLE KQTGAILPPS PKSEITPPPP QPKDRTFPTP IAKPPVFTGK
260 270 280 290 300
DRTEPVTGFQ KAMVKTMSAA LKIPHFGYCD EIDLTQLVKL REELKPVALA
310 320 330 340 350
RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT
360 370 380 390 400
ELGLIVPNVK NVQVRSVFEI AMELNRLQKL GSSGQLGTTD LTGGTFTLSN
410 420 430 440 450
IGSIGGTYAK PVILPPEVAI GALGAIKALP RFDQKGDVYK AQIMNVSWSA
460 470 480
DHRVIDGATM SRFSNLWKSY LENPAFMLLD LK
Length:482
Mass (Da):53,247
Last modified:July 27, 2011 - v2
Checksum:i79E440D1B4B9B948
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti369 – 371EIA → GIG in AAC37681 (PubMed:8605244).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42996 mRNA. Translation: AAC37681.1.
AK165959 mRNA. Translation: BAE38487.1.
CH466532 Genomic DNA. Translation: EDL12381.1.
CCDSiCCDS17787.1.
PIRiS65760.
RefSeqiNP_034152.2. NM_010022.3.
UniGeneiMm.3636.

Genome annotation databases

EnsembliENSMUST00000000349; ENSMUSP00000000349; ENSMUSG00000000340.
GeneIDi13171.
KEGGimmu:13171.
UCSCiuc008rcg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42996 mRNA. Translation: AAC37681.1.
AK165959 mRNA. Translation: BAE38487.1.
CH466532 Genomic DNA. Translation: EDL12381.1.
CCDSiCCDS17787.1.
PIRiS65760.
RefSeqiNP_034152.2. NM_010022.3.
UniGeneiMm.3636.

3D structure databases

ProteinModelPortaliP53395.
SMRiP53395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199061. 6 interactors.
IntActiP53395. 5 interactors.
MINTiMINT-1860345.
STRINGi10090.ENSMUSP00000000349.

PTM databases

iPTMnetiP53395.
PhosphoSitePlusiP53395.
SwissPalmiP53395.

Proteomic databases

EPDiP53395.
MaxQBiP53395.
PaxDbiP53395.
PeptideAtlasiP53395.
PRIDEiP53395.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000349; ENSMUSP00000000349; ENSMUSG00000000340.
GeneIDi13171.
KEGGimmu:13171.
UCSCiuc008rcg.2. mouse.

Organism-specific databases

CTDi1629.
MGIiMGI:105386. Dbt.

Phylogenomic databases

eggNOGiKOG0558. Eukaryota.
COG0508. LUCA.
GeneTreeiENSGT00860000133743.
HOGENOMiHOG000281564.
HOVERGENiHBG104085.
InParanoidiP53395.
KOiK09699.
OMAiTIPHFTY.
OrthoDBiEOG091G0FJ3.
TreeFamiTF314182.

Enzyme and pathway databases

ReactomeiR-MMU-389661. Glyoxylate metabolism and glycine degradation.
R-MMU-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

PROiP53395.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000340.
CleanExiMM_DBT.
ExpressionAtlasiP53395. baseline and differential.
GenevisibleiP53395. 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.
IPR015761. BCKDC_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR23151:SF71. PTHR23151:SF71. 2 hits.
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODB2_MOUSE
AccessioniPrimary (citable) accession number: P53395
Secondary accession number(s): Q3TMF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 139 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, 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.