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Q59098 (ODP2_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Gene names
Name:pdhB
Ordered Locus Names:H16_A1375
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus ›

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 2 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 2 lipoyl-binding domains.

Sequence caution

The sequence AAA21599.1 differs from that shown. Reason: Frameshift at positions 229 and 273.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
Repeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162271

Regions

Domain1 – 7777Lipoyl-binding 1
Domain123 – 19573Lipoyl-binding 2

Sites

Active site5261 Potential

Amino acid modifications

Modified residue441N6-lipoyllysine By similarity
Modified residue1621N6-lipoyllysine By similarity

Experimental info

Sequence conflict2011S → A in AAA21599. Ref.1
Sequence conflict3191F → V in AAA21599. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59098 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 280424CA0475D9E3

FASTA55356,582
        10         20         30         40         50         60 
MSQAIEIKVP DIGDYDAVPV IEVHVKPGDS INAEDALVTL ESDKATMDVP SPQAGVVKDV 

        70         80         90        100        110        120 
RIKVGDNVSE GSVLVMLEAA NEPAAAPAPA AAAPAPAAAA PAPAPAPAAA PAAAPAAGGG 

       130        140        150        160        170        180 
GTIEVKVPDI GDYDAVPVIE VHVKAGDTIN AEDAVVTLES DKATMDVPSP QGGVVKEVKV 

       190        200        210        220        230        240 
KVGDNVAEGT LLLILEGAAA SAAPAAAAAA PAPAASAPAP APAPAAAAPA PAAAPAAAPA 

       250        260        270        280        290        300 
AAGVTGKAAH ASPSVRKFAR ELGVDVSRVP GTGPKGRITQ EDVQGYVKGV MSGQAAAPAQ 

       310        320        330        340        350        360 
AAAAGAGGGE LGLLPWPKFD FTRFGEVESK ALSRIKKISG ANLHRNWVMI PHVTNHDEAD 

       370        380        390        400        410        420 
ITELEAFRLQ LNKENEKSGI KVTMLAFMIK ATVAALKKFP NFNASLDGDN LVLKKYFNIG 

       430        440        450        460        470        480 
FAADTPNGLV VPVIKDADKK GVLEISQEMS ELAKLARDGK LKPDQMQGGC FSISSLGGLG 

       490        500        510        520        530        540 
GTYFTPIINA PEVAIMGVCK SYQKPVWDGK QFAPRLTLPL SLSWDHRVID GAEAARFNTY 

       550 
FGQLLADFRR ILL

« Hide

References

« Hide 'large scale' references
[1]"Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase."
Hein S., Steinbuechel A.
J. Bacteriol. 176:4394-4408(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U09865 Genomic DNA. Translation: AAA21599.1. Frameshift.
AM260479 Genomic DNA. Translation: CAJ92511.1.
PIRB55514.
RefSeqYP_725879.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ59098.
SMRQ59098. Positions 315-553.
ModBaseSearch...

Protein-protein interaction databases

STRING381666.H16_A1375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ92511; CAJ92511; H16_A1375.
GeneID4249767.
KEGGreh:H16_A1375.
PATRIC35232213. VBIRalEut6770_1764.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281562.
KOK00627.
OMACMSISSL.
ProtClustDBPRK11855.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-1372-MONOMER.

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. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. E3_bd. 1 hit.
SSF51230. Hybrid_motif. 2 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_CUPNH
AccessionPrimary (citable) accession number: Q59098
Secondary accession number(s): Q0KBW0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 94 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

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