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Protein

Pyruvate dehydrogenase E1 component subunit alpha

Gene

pdhA

Organism
Acholeplasma laidlawii
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein predictedi

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).

Catalytic activityi

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

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha (EC:1.2.4.1)
Gene namesi
Name:pdhA
OrganismiAcholeplasma laidlawii
Taxonomic identifieri2148 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 345›345Pyruvate dehydrogenase E1 component subunit alphaPRO_0000162197Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

STRINGi441768.ACL_1312.

Structurei

3D structure databases

ProteinModelPortaliP35485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017596. PdhA/BkdA.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03181. PDH_E1_alph_x. 1 hit.

Sequencei

Sequence statusi: Fragment.

P35485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DQNGKVVNEK MEPKLPKETL LKMYKTAVLG RNADIKALQY QRQGRMLTYA
60 70 80 90 100
PNMGQEAAQI GMAAAMEPQD WNSPMYRELN TLLYRGDKLE NVFLYWYGNE
110 120 130 140 150
RGSIKPEGVK ILPTNIIIGS QSNIAAGLAM ASKIRKTNEV TAFTIGDGGT
160 170 180 190 200
AHGEFYEGLN FAASFKAPVV AVIQNNQWAI STPVRKASNS ETLAQKGVAF
210 220 230 240 250
GIPYIQVDGN DMLAMYVASK EAMDRARKGD GPTLIEAFTY RMGPHTTSDD
260 270 280 290 300
PCSIYRTKEE ENEWAKKDQI ARFKTYLINK GYWSEEEDKK LEEEVLAEIN
310 320 330 340
DTFKKVESYG ANVELIEIFE HTYAEMTPQL KEQYEEHKKY LEGVK
Length:345
Mass (Da):38,962
Last modified:June 1, 1994 - v1
Checksum:i797F9F67DE0C2995
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81753 Genomic DNA. Translation: AAA21907.1.
PIRiA42653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81753 Genomic DNA. Translation: AAA21907.1.
PIRiA42653.

3D structure databases

ProteinModelPortaliP35485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi441768.ACL_1312.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017596. PdhA/BkdA.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03181. PDH_E1_alph_x. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii."
    Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.
    J. Bacteriol. 174:1388-1396(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiODPA_ACHLA
AccessioniPrimary (citable) accession number: P35485
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 24, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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.