SubmitCancel

Skip Header

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

P81896

- ODO2_SOLTU

UniProt

P81896 - ODO2_SOLTU

(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

Dihydrolipoamide-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).1 Publication

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.1 Publication

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.By similarity

Pathwayi

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoamide-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
E2K
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

Mitochondrion membrane 1 Publication

GO - Cellular componenti

  1. mitochondrial membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›20›20Dihydrolipoamide-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000238929Add
BLAST

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.By similarity

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Lipoyl

Sequencei

Sequence statusi: Fragment.

P81896-1 [UniParc]FASTAAdd to Basket

« Hide

XSNSGDLVDA VVPYMGESIS                                    20
Length:20
Mass (Da):2,051
Last modified:June 1, 2000 - v1
Checksum:i9256BE292E26A344
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei20 – 201

Cross-referencesi

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and characterization in potato."
    Millar A.H., Hill S.A., Leaver C.J.
    Biochem. J. 343:327-334(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Strain: cv. Romano.
    Tissue: Tuber.

Entry informationi

Entry nameiODO2_SOLTU
AccessioniPrimary (citable) accession number: P81896
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2000
Last modified: February 19, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3