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Q9I3D2 (ODO2_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:sucB
Ordered Locus Names:PA1586
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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) By similarity.

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.

Subunit structure

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

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000287784

Regions

Domain1 – 7676Lipoyl-binding

Sites

Active site3801 Potential
Active site3841 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q9I3D2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 01FCCEB71E04353C

FASTA40942,887
        10         20         30         40         50         60 
MAIEIKAPTF PESVADGTVA TWHKKPGEAV KRDELIVDIE TDKVVIEVLA EADGVLAEII 

        70         80         90        100        110        120 
KNEGDTVLSN ELLGKLNEGG AAAPAAPAAA APAAAPAAQA AAPAAAGGDD AILSPAARKL 

       130        140        150        160        170        180 
AEEAGIDPNS IAGTGKGGRV TKEDVVAAVE AKKNAPAAPA KPAAPAAEAP IFAAGDRVEK 

       190        200        210        220        230        240 
RVPMTRLRAK VAERLVEAQS AMAMLTTFNE VNMKPIMDLR SKYKDLFEKK HNGVRLGFMS 

       250        260        270        280        290        300 
FFVKAATEAL KRFPGVNASI DGNDIVYHGY QDIGVAVSSD RGLVVPVLRN AEFMSLAEIE 

       310        320        330        340        350        360 
GGIANFGKKA KEGKLTIEDM TGGTFTISNG GVFGSLLSTP IVNPPQTAIL GMHKIQERPM 

       370        380        390        400 
AVNGQVVILP MMYLALSYDH RLIDGKEAVS FLVAIKDLLE DPARLLLDV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG04975.1.
PIRH83448.
RefSeqNP_250277.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9I3D2.
SMRQ9I3D2. Positions 2-80, 112-147, 177-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA1586.

Proteomic databases

PRIDEQ9I3D2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID881930.
KEGGpae:PA1586.
PATRIC19837518. VBIPseAer58763_1645.

Organism-specific databases

PseudoCAPPA1586.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
KOK00658.
OMAATFGKKA.
OrthoDBEOG610413.
ProtClustDBPRK05704.

Enzyme and pathway databases

UniPathwayUPA00868; UER00840.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
IPR006255. SucB.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODO2_PSEAE
AccessionPrimary (citable) accession number: Q9I3D2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways