Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P10801

- ODP1_AZOVI

UniProt

P10801 - ODP1_AZOVI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pyruvate dehydrogenase E1 component

Gene
N/A
Organism
Azotobacter vinelandii
Status
Reviewed - 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

Thiamine pyrophosphate.

GO - Molecular functioni

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

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
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 (EC:1.2.4.1)
OrganismiAzotobacter vinelandii
Taxonomic identifieri354 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 45›45Pyruvate dehydrogenase E1 componentPRO_0000162239Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP10801.
SMRiP10801. Positions 1-42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
InterProiIPR009014. Transketo_C/Pyr-ferredox_oxred.
[Graphical view]
SUPFAMiSSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Fragment.

P10801 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40
EVDRYWVVLA ALEALADRGD IEAKVVAEAI AKFGIDPDKR NPLDC
Length:45
Mass (Da):4,957
Last modified:July 1, 1989 - v1
Checksum:iC2929BB637D1B032
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12455 Genomic DNA. Translation: CAA30986.1.
PIRiS12208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12455 Genomic DNA. Translation: CAA30986.1 .
PIRi S12208.

3D structure databases

ProteinModelPortali P10801.
SMRi P10801. Positions 1-42.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
InterProi IPR009014. Transketo_C/Pyr-ferredox_oxred.
[Graphical view ]
SUPFAMi SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis."
    Hanemaaijer R., Janssen A., de Kok A., Veeger C.
    Eur. J. Biochem. 174:593-599(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.

Entry informationi

Entry nameiODP1_AZOVI
AccessioniPrimary (citable) accession number: P10801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program