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P20708 (ODO2_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:odhB
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently.

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.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processL-lysine catabolic process to acetyl-CoA via saccharopine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentoxoglutarate dehydrogenase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondihydrolipoyllysine-residue succinyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 399398Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
PRO_0000162255

Regions

Domain2 – 7675Lipoyl-binding

Sites

Active site3701 By similarity
Active site3741 By similarity

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Secondary structure

............... 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20708 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3A801A1B519E73D3

FASTA39942,003
        10         20         30         40         50         60 
MAIDIKAPTF PESIADGTVA TWHKKPGEPV KRDELIVDIE TDKVVMEVLA EADGVIAEIV 

        70         80         90        100        110        120 
KNEGDTVLSG ELLGKLTEGG AATAAPAAAP APAAAAPAAA EAPILSPAAR KIAEENAIAA 

       130        140        150        160        170        180 
DSITGTGKGG RVTKEDAVAA AEAKKSAPAG QPAPAATAAP LFAAGDRVEK RVPMTRLRAK 

       190        200        210        220        230        240 
VAERLVEAQS SMAMLTTFNE VNMKPVMELR AKYKDLFEKT HNGVRLGFMS FFVKAAVEAL 

       250        260        270        280        290        300 
KRQPGVNASI DGNDIVYHGY QDIGVAVSSD RGLVVPVLRN AEFMSLAEIE GGINEFGKKA 

       310        320        330        340        350        360 
KAGKLTIEEM TGGTFTISNG GVFGSLLSTP IVNPPQTAIL GMHKIQERPM AVNGQVVILP 

       370        380        390 
MMYLALSYDH RLIDGKEAVT FLVTMKDLLE DPARLLLDV 

« Hide

References

[1]"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component."
Westphal A.H., de Kok A.
Eur. J. Biochem. 187:235-239(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
[2]"Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene."
Westphal A.H., de Kok A.
Eur. J. Biochem. 172:299-305(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-399.
Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
[3]"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component."
Schulze E., Westphal A.H., Hanemaaijer R., de Kok A.
Eur. J. Biochem. 187:229-234(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
[4]"Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Evidence for high structural similarity with the lipoyl domain of the pyruvate dehydrogenase complex."
Berg A., Smits O., de Kok A., Vervoort J.
Eur. J. Biochem. 234:148-159(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-80.
[5]"Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii."
Berg A., Vervoort J., de Kok A.
J. Mol. Biol. 261:432-442(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-78.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37307 Genomic DNA. Translation: AAA22138.1. Sequence problems.
X52432 Genomic DNA. Translation: CAA36678.1.
X52433 Genomic DNA. Translation: CAA36681.1.
PIRS07779.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GHJNMR-A2-80[»]
1GHKNMR-A2-80[»]
ProteinModelPortalP20708.
SMRP20708. Positions 2-80, 167-399.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP20708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.61. 49.
SABIO-RKP20708.
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...

Other

EvolutionaryTraceP20708.

Entry information

Entry nameODO2_AZOVI
AccessionPrimary (citable) accession number: P20708
Secondary accession number(s): Q44474
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 103 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways