Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P10802 (ODP2_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 109. 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 acetyltransferase component of pyruvate dehydrogenase complex

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactor

Binds 3 lipoyl cofactors covalently By similarity.

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 3 lipoyl-binding domains.

Sequence caution

The sequence CAA30987.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
Repeat
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentpyruvate dehydrogenase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 638637Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162272

Regions

Domain2 – 7372Lipoyl-binding 1
Domain118 – 19073Lipoyl-binding 2
Domain223 – 29573Lipoyl-binding 3
Region328 – 38154E1/E3 binding
Region382 – 638257Catalytic

Sites

Active site6111 Potential

Amino acid modifications

Modified residue401N6-lipoyllysine Potential
Modified residue1571N6-lipoyllysine Potential
Modified residue2621N6-lipoyllysine Potential

Secondary structure

............................................................. 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10802 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8B92CB5ADEA0BEA1

FASTA63865,045
        10         20         30         40         50         60 
MSEIIRVPDI GGDGEVIELL VKTGDLIEVE QGLVVLESAK ASMEVPSPKA GVVKSVSVKL 

        70         80         90        100        110        120 
GDKLKEGDAI IELEPAAGAA AAPAEAAAVP AAPTQAVDEA EAPSPGASAT PAPAAASQEV 

       130        140        150        160        170        180 
RVPDIGSAGK ARVIEVLVKA GDQVQAEQSL IVLESDKASM EIPSPASGVV ESVAIQLNAE 

       190        200        210        220        230        240 
VGTGDLILTL RTTGAQAQPT APAAAAAASP APAPLAPAAA GPQEVKVPDI GSAGKARVIE 

       250        260        270        280        290        300 
VLVKAGDQVQ AEQSLIVLES DKASMEIPSP AAGVVESVAV QLNAEVGTGD QILTLRVAGA 

       310        320        330        340        350        360 
APSGPRARGS PGQAAAAPGA APAPAPVGAP SRNGAKVHAG PAVRQLAREF GVELAAINST 

       370        380        390        400        410        420 
GPRGRILKED VQAYVKAMMQ KAKEAPAAGA ASGAGIPPIP PVDFAKYGEI EEVPMTRLMQ 

       430        440        450        460        470        480 
IGATNLHRSW LNVPHVTQFE SADITELEAF RVAQKAVAEK AGVKLTVLPL LLKACAYLLK 

       490        500        510        520        530        540 
ELPDFNSSLA PSGQALIRKK YVHIGFAVDT PDGLLVPVIR NVDQKSLLQL AAEAAELAEK 

       550        560        570        580        590        600 
ARSKKLGADA MQGACFTISS LGHIGGTAFT PIVNAPEVAI LGVSKASMQP VWDGKAFQPR 

       610        620        630 
LMLPLSLSYD HRVINGAAAA RFTKRLGDLL ADIRAILL 

« Hide

References

[1]"The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis."
Hanemaaijer R., Janssen A., de Kok A., Veeger C.
Eur. J. Biochem. 174:593-599(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
[2]"The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
Hanemaaijer R., de Kok A., Jolles J., Veeger C.
Eur. J. Biochem. 169:245-252(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16 AND 381-416.
[3]"Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2-oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy."
Hanemaaijer R., Vervoort J., Westphal A.H., de Kok A., Veeger C.
FEBS Lett. 240:205-210(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: LIPOYL DOMAIN CONFORMATION.
[4]"Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex."
Mattevi A., Obmolova G., Schulze E., Kalk K.H., Westphal A.H., de Kok A., Hol W.G.J.
Science 255:1544-1550(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 382-638.
[5]"Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
Berg A., de Kok A., Vervoort J.
Eur. J. Biochem. 221:87-100(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-79.
[6]"Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
Berg A., Vervoort J., de Kok A.
Eur. J. Biochem. 244:352-360(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-79.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12455 Genomic DNA. Translation: CAA30987.1. Different initiation.
PIRXXAV. S01017.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DPBX-ray2.50A396-637[»]
1DPCX-ray2.60A396-637[»]
1DPDX-ray2.70A396-637[»]
1EAAX-ray2.60A396-637[»]
1EABX-ray2.60A396-637[»]
1EACX-ray2.60A396-637[»]
1EADX-ray2.60A396-637[»]
1EAEX-ray2.60A396-637[»]
1EAFX-ray2.60A396-637[»]
1IYUNMR-A2-79[»]
1IYVNMR-A2-79[»]
ProteinModelPortalP10802.
SMRP10802. Positions 2-79, 396-638.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10802.

Entry information

Entry nameODP2_AZOVI
AccessionPrimary (citable) accession number: P10802
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 109 of the entry and version 3 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