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P31051

- ODO2_PSEPU

UniProt

P31051 - ODO2_PSEPU

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Protein

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene

sucB

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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).

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei29 – 291By similarity
Active sitei33 – 331By similarity

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:
Dihydrolipoyllysine-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
Gene namesi
Name:sucB
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 58›58Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexPRO_0000162265Add
BLAST

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Structurei

3D structure databases

ProteinModelPortaliP31051.
SMRiP31051. Positions 1-58.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.Curated

Keywords - Domaini

Lipoyl

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P31051-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHNIIQRPMA INGQVVIRPM MYLALSYDHR LIDGKEAVTF LVTIKNLLED

PSRLLLDI
Length:58
Mass (Da):6,691
Last modified:October 1, 1996 - v2
Checksum:i36EC244AA98374E3
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M80189 Genomic DNA. Translation: AAA96436.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M80189 Genomic DNA. Translation: AAA96436.1 .

3D structure databases

ProteinModelPortali P31051.
SMRi P31051. Positions 1-58.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
InterProi IPR001078. 2-oxoacid_DH_actylTfrase.
IPR023213. CAT-like_dom.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida."
    Palmer J.A., Hatter K., Sokatch J.R.
    J. Bacteriol. 173:3109-3116(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: G2.
  2. Sokatch J.R.
    Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiODO2_PSEPU
AccessioniPrimary (citable) accession number: P31051
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3