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A5A6L0

- ODPA_PANTR

UniProt

A5A6L0 - ODPA_PANTR

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Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Thiamine pyrophosphate.By similarity

Enzyme regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.By similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
  2. pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  2. glucose metabolic process Source: UniProtKB-KW
  3. glycolytic process Source: InterPro
  4. tricarboxylic acid cycle Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC:1.2.4.1)
Alternative name(s):
PDHE1-A type I
Gene namesi
Name:PDHA1
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
ProteomesiUP000002277: Unplaced

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
  2. pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionBy similarityAdd
BLAST
Chaini30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialPRO_0000297491Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-acetyllysine; alternateBy similarity
Modified residuei63 – 631N6-succinyllysine; alternateBy similarity
Modified residuei232 – 2321Phosphoserine; by PDK1By similarity
Modified residuei244 – 2441N6-acetyllysine; alternateBy similarity
Modified residuei244 – 2441N6-succinyllysine; alternateBy similarity
Modified residuei277 – 2771N6-succinyllysineBy similarity
Modified residuei293 – 2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei300 – 3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
Modified residuei301 – 3011PhosphotyrosineBy similarity
Modified residuei313 – 3131N6-acetyllysine; alternateBy similarity
Modified residuei313 – 3131N6-succinyllysine; alternateBy similarity
Modified residuei321 – 3211N6-acetyllysineBy similarity
Modified residuei336 – 3361N6-acetyllysineBy similarity
Modified residuei385 – 3851N6-succinyllysineBy similarity

Post-translational modificationi

Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation (By similarity).By similarity
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiA5A6L0.

Interactioni

Subunit structurei

Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is 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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliA5A6L0.
SMRiA5A6L0. Positions 29-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiA5A6L0.
KOiK00161.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A5A6L0-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP
60 70 80 90 100
PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC
110 120 130 140 150
CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG
160 170 180 190 200
GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN
210 220 230 240 250
QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP
260 270 280 290 300
GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSGPGVS
310 320 330 340 350
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA
360 370 380 390
QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
Length:390
Mass (Da):43,238
Last modified:June 12, 2007 - v1
Checksum:i4F95746CBB792E78
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB222138 mRNA. Translation: BAF62383.1.
RefSeqiNP_001104283.1. NM_001110813.1.
UniGeneiPtr.3278.

Genome annotation databases

GeneIDi465525.
KEGGiptr:465525.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB222138 mRNA. Translation: BAF62383.1 .
RefSeqi NP_001104283.1. NM_001110813.1.
UniGenei Ptr.3278.

3D structure databases

ProteinModelPortali A5A6L0.
SMRi A5A6L0. Positions 29-390.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi A5A6L0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 465525.
KEGGi ptr:465525.

Organism-specific databases

CTDi 5160.

Phylogenomic databases

eggNOGi COG1071.
HOGENOMi HOG000281336.
HOVERGENi HBG001863.
InParanoidi A5A6L0.
KOi K00161.

Miscellaneous databases

NextBioi 20843882.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome."
    Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.
    Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.

Entry informationi

Entry nameiODPA_PANTR
AccessioniPrimary (citable) accession number: A5A6L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 12, 2007
Last modified: October 29, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3