Reviewed, UniProtKB/Swiss-Prot Q8BMF4 (ODP2_MOUSE)

Names and origin

Protein names

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 names

Name:

Dlat

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Subunit structure	20 to 30 alpha(2)-beta2 tetramers of E1 + 6 homodimers of E3 + 60 copies of E2 By similarity.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Lipoyl Repeat Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	acetyl-CoA biosynthetic process from pyruvate Ref.3 Inferred by curator. Source: MGI glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial pyruvate dehydrogenase complex Ref.3 Traceable author statement. Source: MGI
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Ref.3 Traceable author statement. Source: MGI lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 85	85	Mitochondrion By similarity
	Chain	86 – 642	557	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial		PRO_0000285717
Regions
	Domain	91 – 165	75	Lipoyl-binding 1
	Domain	218 – 292	75	Lipoyl-binding 2
	Region	353 – 384	32	E3- and/or E1-component binding domain Potential
	Region	466 – 642	177	Catalytic By similarity
	Region	610 – 621	12	CoA-binding By similarity
Sites
	Active site	615	1	Potential
	Active site	619	1	Potential
Amino acid modifications
	Modified residue	258	1	N6-lipoyllysine By similarity
	Modified residue	461	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	84	1	S → Y in AAL02400. Ref.3
	Sequence conflict	198	1	P → T in BAC27715. Ref.1
	Sequence conflict	225	1	L → P in AAL02400. Ref.3
	Sequence conflict	393	1	A → V in AAH31495. Ref.2
	Sequence conflict	604	1	A → V in AAH31495. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8BMF4-1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 1294FAC4857FC29C	FASTA	642	67,942
	10 20 30 40 50 60 MWRVCARRAR SAVPRDGFRA RWAALKEGPG APCGSPRIGP AAVRCGSGIP RYGVRSLCGW 70 80 90 100 110 120 SSGSGTVPRN RLLRQLLGSP SRRSYSLPPH QKVPLPSLSP TMQAGTIARW EKKEGEKISE 130 140 150 160 170 180 GDLIAEVETD KATVGFESLE ECYMAKILVP EGTRDVPVGS IICITVEKPQ DIEAFKNYTL 190 200 210 220 230 240 DLAAAAAPQA APAAAPAPAA APAAPSASAP GSSYPTHMQI VLPALSPTMT MGTVQRWEKK 250 260 270 280 290 300 VGEKLSEGDL LAEIETDKAT IGFEVQEEGY LAKILVPEGT RDVPLGAPLC IIVEKQEDIA 310 320 330 340 350 360 AFADYRPTEV TSLKPQAAPP APPPVAAVPP TPQPVAPTPS AAPAGPKGRV FVSPLAKKLA 370 380 390 400 410 420 AEKGIDLTQV KGTGPEGRII KKDIDSFVPS KAAPAAAAAM APPGPRVAPA PAGVFTDIPI 430 440 450 460 470 480 SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG EVLLVRKELN KMLEGKGKIS VNDFIIKASA 490 500 510 520 530 540 LACLKVPEAN SSWMDTVIRQ NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA 550 560 570 580 590 600 SKAREGKLQP HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG 610 620 630 640 FDVASVMSVT LSCDHRVVDG AVGAQWLAEF KKYLEKPITM LL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Medulla oblongata.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II, FVB/N-3 and NMRI. Tissue: Mammary tumor.
[3]	"Molecular cloning, and characterization and expression of dihydrolipoamide acetyltransferase component of murine pyruvate dehydrogenase complex in bile duct cancer cells." Wang L., Kaneko S., Kagaya M., Ohno H., Honda M., Kobayashi K. J. Gastroenterol. 37:449-454(2002) [PubMed: 12108679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-642. Tissue: Hepatoma.
[4]	Lubec G., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 93-109; 147-176; 282-295; 383-424; 469-477; 486-499; 528-542; 548-569; 600-631 AND 633-642, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00153660.
RefSeq	NP_663589.3.
UniGene	Mm.285076 Mm.471144
3D structure databases
HSSP	HSSP built from PDB template 1FYC based on UniProtKB P10515.
SMR	Q8BMF4. Positions 91-181, 213-314, 347-395, 404-642.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BMF4.
Proteomic databases
PRIDE	Q8BMF4.
Genome annotation databases
Ensembl	ENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168; Mus musculus. [Genome view]
GeneID	235339.
KEGG	mmu:235339.
Organism-specific databases
CTD	235339.
MGI	MGI:2385311. Dlat.
Phylogenomic databases
eggNOG	roNOG14419.
HOGENOM	HBG630916.
HOVERGEN	Q8BMF4.
InParanoid	Q8BMF4.
OMA	GKLLCII.
OrthoDB	EOG9NCPZ1.
PhylomeDB	Q8BMF4.
Enzyme and pathway databases
BRENDA	2.3.1.12. 244.
Gene expression databases
ArrayExpress	Q8BMF4.
Bgee	Q8BMF4.
Genevestigator	Q8BMF4.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. IPR011053. Single_hybrid_motif. [Graphical view]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	382617.
SOURCE	Search...

Entry information

Entry name

ODP2_MOUSE

Accession

Primary (citable) accession number: Q8BMF4
Secondary accession number(s): Q8K2G8, Q8R339, Q91ZB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	May 1, 2007
Last modified:	February 9, 2010
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)