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P53395 (ODB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Dbt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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).

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry.

Subcellular location

Mitochondrion matrix.

Miscellaneous

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.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6161Mitochondrion Potential
Chain62 – 482421Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
PRO_0000020490

Regions

Domain65 – 13874Lipoyl-binding

Sites

Active site4521 Potential
Active site4561 Potential

Amino acid modifications

Modified residue1051N6-lipoyllysine By similarity
Modified residue2951N6-acetyllysine By similarity

Experimental info

Sequence conflict369 – 3713EIA → GIG in AAC37681. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P53395 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 79E440D1B4B9B948

FASTA48253,247
        10         20         30         40         50         60 
MAAARVLRTW SQNAVRLTCV RYFQTFNSAR VLKPKCVCSV GYPLFKYSQP RHSLRTAAVL 

        70         80         90        100        110        120 
QGQVVQFKLS DIGEGIREVT IKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKR 

       130        140        150        160        170        180 
LYYNLDDIAY VGKPLIDIET EALKDSEEDV VETPAVSHDE HTHQEIKGQK TLATPAVRRL 

       190        200        210        220        230        240 
AMENNIKLSE VVGSGKDGRI LKEDILSFLE KQTGAILPPS PKSEITPPPP QPKDRTFPTP 

       250        260        270        280        290        300 
IAKPPVFTGK DRTEPVTGFQ KAMVKTMSAA LKIPHFGYCD EIDLTQLVKL REELKPVALA 

       310        320        330        340        350        360 
RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT ELGLIVPNVK 

       370        380        390        400        410        420 
NVQVRSVFEI AMELNRLQKL GSSGQLGTTD LTGGTFTLSN IGSIGGTYAK PVILPPEVAI 

       430        440        450        460        470        480 
GALGAIKALP RFDQKGDVYK AQIMNVSWSA DHRVIDGATM SRFSNLWKSY LENPAFMLLD 


LK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42996 mRNA. Translation: AAC37681.1.
AK165959 mRNA. Translation: BAE38487.1.
CH466532 Genomic DNA. Translation: EDL12381.1.
IPIIPI00130535.
PIRS65760.
RefSeqNP_034152.2. NM_010022.3.
UniGeneMm.3636.

3D structure databases

ProteinModelPortalP53395.
SMRP53395. Positions 62-147, 165-213, 249-482.
ModBaseSearch...

Protein-protein interaction databases

IntActP53395. 2 interactions.
STRING10090.ENSMUSP00000000349.

PTM databases

PhosphoSiteP53395.

Proteomic databases

PaxDbP53395.
PRIDEP53395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000349; ENSMUSP00000000349; ENSMUSG00000000340.
GeneID13171.
KEGGmmu:13171.

Organism-specific databases

CTD1629.
MGIMGI:105386. Dbt.

Phylogenomic databases

eggNOGCOG0508.
GeneTreeENSGT00560000077144.
HOGENOMHOG000281564.
HOVERGENHBG104085.
InParanoidQ3TMF5.
KOK09699.
OMAAREEHTH.
OrthoDBEOG4PRSQK.

Gene expression databases

BgeeP53395.
CleanExMM_DBT.
GenevestigatorP53395.
GermOnlineENSMUSG00000000340. Mus musculus.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR015761. Lip_Acyl_TA.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERPTHR23151:SF11. PTHR23151:SF11. 1 hit.
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. E3_bd. 1 hit.
SSF51230. Hybrid_motif. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283268.
SOURCESearch...

Entry information

Entry nameODB2_MOUSE
AccessionPrimary (citable) accession number: P53395
Secondary accession number(s): Q3TMF5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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