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: 5 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei452 – 4521Sequence Analysis
Active sitei456 – 4561Sequence Analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_305961. 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
ProteomesiUP000000589 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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6161MitochondrionSequence AnalysisAdd
BLAST
Chaini62 – 482421Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialPRO_0000020490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-lipoyllysinePROSITE-ProRule annotationBy similarity
Modified residuei133 – 1331N6-succinyllysine1 Publication
Modified residuei196 – 1961N6-acetyllysine; alternate1 Publication
Modified residuei196 – 1961N6-succinyllysine; alternate1 Publication
Modified residuei202 – 2021N6-acetyllysine1 Publication
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei243 – 2431N6-acetyllysine1 Publication
Modified residuei250 – 2501N6-acetyllysine1 Publication
Modified residuei261 – 2611N6-succinyllysine1 Publication
Modified residuei289 – 2891N6-acetyllysine; alternate1 Publication
Modified residuei289 – 2891N6-succinyllysine; alternate1 Publication
Modified residuei295 – 2951N6-acetyllysine1 Publication
Modified residuei304 – 3041N6-acetyllysine1 Publication
Modified residuei435 – 4351N6-acetyllysine1 Publication
Modified residuei440 – 4401N6-acetyllysine; alternate1 Publication
Modified residuei440 – 4401N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53395.
PaxDbiP53395.
PRIDEiP53395.

PTM databases

PhosphoSiteiP53395.

Expressioni

Gene expression databases

BgeeiP53395.
CleanExiMM_DBT.
GenevisibleiP53395. MM.

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Protein-protein interaction databases

BioGridi199061. 4 interactions.
IntActiP53395. 5 interactions.
MINTiMINT-1860345.
STRINGi10090.ENSMUSP00000000349.

Structurei

3D structure databases

ProteinModelPortaliP53395.
SMRiP53395. Positions 62-147, 165-213, 249-482.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 13976Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG0508.
GeneTreeiENSGT00790000123041.
HOGENOMiHOG000281564.
HOVERGENiHBG104085.
InParanoidiP53395.
KOiK09699.
OMAiATDTDNG.
OrthoDBiEOG7GFB4W.
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:SF46. PTHR23151:SF46. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti369 – 3713EIA → GIG in AAC37681 (PubMed:8605244).Curated

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. Positions 62-147, 165-213, 249-482.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199061. 4 interactions.
IntActiP53395. 5 interactions.
MINTiMINT-1860345.
STRINGi10090.ENSMUSP00000000349.

PTM databases

PhosphoSiteiP53395.

Proteomic databases

MaxQBiP53395.
PaxDbiP53395.
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

eggNOGiCOG0508.
GeneTreeiENSGT00790000123041.
HOGENOMiHOG000281564.
HOVERGENiHBG104085.
InParanoidiP53395.
KOiK09699.
OMAiATDTDNG.
OrthoDBiEOG7GFB4W.
TreeFamiTF314182.

Enzyme and pathway databases

ReactomeiREACT_305961. Branched-chain amino acid catabolism.

Miscellaneous databases

NextBioi283268.
PROiP53395.
SOURCEiSearch...

Gene expression databases

BgeeiP53395.
CleanExiMM_DBT.
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:SF46. PTHR23151:SF46. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the murine branched chain alpha-ketoacid dehydrogenase E2 subunit: presence of 3' B1 repeat elements."
    Costeas P.A., Tonelli L.A., Chinsky J.M.
    Biochim. Biophys. Acta 1305:25-28(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-196; LYS-261; LYS-289 AND LYS-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196; LYS-202; LYS-243; LYS-250; LYS-289; LYS-295; LYS-304; LYS-435 AND LYS-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: June 24, 2015
This is version 125 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

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.