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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: Annotation score: 4 out of 5-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 N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(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

GO - Cellular componenti

  • mitochondrial pyruvate dehydrogenase complex Source: PomBase
  • mitochondrion Source: PomBase

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.
PRIDEiO59816.

Interactioni

Protein-protein interaction databases

BioGridi275378. 4 interactors.
MINTiMINT-4676403.

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.
OMAiPHGRIQA.
OrthoDBiEOG092C32CQ.
PhylomeDBiO59816.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiView protein in InterPro
IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR006257. LAT1.
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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliO59816.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275378. 4 interactors.
MINTiMINT-4676403.

Proteomic databases

MaxQBiO59816.
PRIDEiO59816.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPCC794.07.
PomBaseiSPCC794.07. lat1.

Phylogenomic databases

HOGENOMiHOG000281566.
InParanoidiO59816.
KOiK00627.
OMAiPHGRIQA.
OrthoDBiEOG092C32CQ.
PhylomeDBiO59816.

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.

Miscellaneous databases

PROiPR:O59816.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiView protein in InterPro
IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR006257. LAT1.
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.
ProtoNetiSearch...

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: May 10, 2017
This is version 130 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

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.