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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: -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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi: L-lysine degradation via saccharopine pathway

This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (AB688_19495), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (BGP82_17630), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (BGP80_11835), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (BGP84_08660), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (B8W72_07160), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (QV12_19365), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (BL240_19240), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (AYO28_10145), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (SAMN03097715_00103), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (A3K88_10365), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (A3L25_25165), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (PU99_23635), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (B7H17_04120), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (CRX57_24285), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (HA62_00660), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (HB4184_15790), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (AWT69_001598), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (B7H19_15155), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (KF715C_ch41370), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (B7H18_28670), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (AYO08_18350), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (kgdB), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (CR511_18800), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (A6E19_12355), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (DW66_4032), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (sucB)
This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei29By similarity1
Active sitei33By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayi
UPA00868;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)DescriptionActionsGraphical viewLength
ChainiPRO_0000162265‹1 – 58Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complexAdd BLAST›58

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.

Structurei

3D structure databases

ProteinModelPortaliP31051
SMRiP31051
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA

Family and domain databases

Gene3Di3.30.559.10, 1 hit
InterProiView protein in InterPro
IPR001078 2-oxoacid_DH_actylTfrase
IPR023213 CAT-like_dom_sf
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit

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)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80189 Genomic DNA Translation: AAA96436.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80189 Genomic DNA Translation: AAA96436.1

3D structure databases

ProteinModelPortaliP31051
SMRiP31051
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C7S Bacteria
COG0508 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00868;UER00840

Family and domain databases

Gene3Di3.30.559.10, 1 hit
InterProiView protein in InterPro
IPR001078 2-oxoacid_DH_actylTfrase
IPR023213 CAT-like_dom_sf
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiODO2_PSEPU
AccessioniPrimary (citable) accession number: P31051
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 86 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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