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

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

lat1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).

Miscellaneous

The E2 component contains covalently-bound lipoyl cofactors and it participates in the generation of acetyl groups from hydroxyethyl-thiamine pyrophosphate-E1 and their transfer to coenzyme A.

Catalytic activityi

Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei456Sequence analysis1
Active sitei460Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-SPO-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-SPO-389661 Glyoxylate metabolism and glycine degradation
R-SPO-5362517 Signaling by Retinoic Acid
R-SPO-70268 Pyruvate metabolism

Names & Taxonomyi

Protein namesi
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 namesi
Name:lat1
ORF Names:SPCC794.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC794.07
PomBaseiSPCC794.07 lat1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 28MitochondrionBy similarityAdd BLAST28
ChainiPRO_000002048229 – 483Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialAdd BLAST455

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei94N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

MaxQBiO59816
PaxDbiO59816
PRIDEiO59816

PTM databases

iPTMnetiO59816

Interactioni

Protein-protein interaction databases

BioGridi275378, 4 interactors
STRINGi4896.SPCC794.07.1

Structurei

3D structure databases

ProteinModelPortaliO59816
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 129Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST77
Domaini187 – 224Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

HOGENOMiHOG000281566
InParanoidiO59816
KOiK00627
OMAiTMEFESF
OrthoDBiEOG092C32CQ
PhylomeDBiO59816

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

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

O59816-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSANMLRRM HHGVAVTRML LVSNGKVQVK KSALYPVMAK LARTYATKNY
60 70 80 90 100
PAHTVINMPA LSPTMTTGNI GAFQKKIGDK IEPGDVLCEI ETDKAQIDFE
110 120 130 140 150
QQDEGYLAKI LIETGTKDVP VGKPLAVTVE NEGDVAAMAD FTIEDSSAKE
160 170 180 190 200
PSAKSGEEKS APSSEKQSKE TSSPSNVSGE ERGDRVFASP LARKLAEEKD
210 220 230 240 250
LDLSQIRGSG PNGRIIKVDI ENFKPVVAPK PSNEAAAKAT TPAASAADAA
260 270 280 290 300
APGDYEDLPL SNMRKIIASR LAESKNMNPH YYVTVSVNME KIIRLRAALN
310 320 330 340 350
AMADGRYKLS VNDLVIKATT AALRQVPEVN AAWMGDFIRQ YKNVDISMAV
360 370 380 390 400
ATPSGLITPV IRNTHALGLA EISTLAKDYG QRARNNKLKP EEYQGGTFTI
410 420 430 440 450
SNLGMFPVDQ FTAIINPPQA CILAVGTTVD TVVPDSTSEK GFKVAPIMKC
460 470 480
TLSSDHRVVD GAMAARFTTA LKKILENPLE IML
Length:483
Mass (Da):52,061
Last modified:August 1, 1998 - v1
Checksum:i7E4B6340665932F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA Translation: CAA19134.1
PIRiT41615
RefSeqiNP_587755.1, NM_001022748.2

Genome annotation databases

EnsemblFungiiSPCC794.07.1; SPCC794.07.1:pep; SPCC794.07
GeneIDi2538797
KEGGispo:SPCC794.07

Similar proteinsi

Entry informationi

Entry nameiODP2_SCHPO
AccessioniPrimary (citable) accession number: O59816
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: March 28, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health