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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

DLAT

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei192 – 1921Sequence AnalysisBy similarity
Active sitei196 – 1961Sequence AnalysisBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialBy similarity (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complexBy similarity
Pyruvate dehydrogenase complex component E2By similarity
Short name:
PDC-E2By similarity
Short name:
PDCE2By similarity
Gene namesi
Name:DLATBy similarity
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

  • Mitochondrion matrix By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 219›219Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000394399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211N6-succinyllysineBy similarity

Proteomic databases

PRIDEiP86197.

Expressioni

Tissue specificityi

Detected at higher levels in cauda epididymal spermatazoa than in caput epididymal spermatazoa (at protein level).1 Publication

Interactioni

Subunit structurei

Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (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 (By similarity).By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini‹1 – ›17›17Lipoyl-binding 1By similarityAdd
BLAST
Domaini‹18 – 28›11Lipoyl-binding 2By similarityAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 5721E3- and/or E1-component binding domainSequence AnalysisBy similarityAdd
BLAST
Regioni187 – 19812CoA-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Sequence Analysis
Contains 2 lipoyl-binding domains.Sequence Analysis

Keywords - Domaini

Lipoyl, Repeat

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragments.

P86197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VPLPSLSPTM QAGTIARDVP LGAPLCIIVE KGRVFVSPLA KGIDLTQVKG
60 70 80 90 100
TGPEGDIDSF VPSKVPEANS SWMDTVIRQN HVVDVSVAVS TPAGLITPIV
110 120 130 140 150
FNAHIKGLET IASDVVSLAS KEGKLQPHEF QGGTFTISNL GMFGIKNFSA
160 170 180 190 200
IINPPQACIL AIGASEDKLI PADNEKGFDV ASVMSVTLSC DHRVVDGAVG
210
AQWLAEFKKY LEKPITMLL
Length:219
Mass (Da):23,117
Last modified:June 15, 2010 - v1
Checksum:i11B4C4C826FE3B08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi17 – 182Curated
Non-adjacent residuesi31 – 322Curated
Non-adjacent residuesi40 – 412Curated
Non-adjacent residuesi55 – 562Curated
Non-adjacent residuesi63 – 642Curated
Non-adjacent residuesi121 – 1222Curated

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP86197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
    Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
    Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

Entry informationi

Entry nameiODP2_MESAU
AccessioniPrimary (citable) accession number: P86197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: June 24, 2015
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. 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.