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O66119 (ODP2_ZYMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. 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:pdhC
Synonyms:pdhB
Ordered Locus Names:ZMO0510
OrganismZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) [Complete proteome] [HAMAP]
Taxonomic identifier264203 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas ›

Protein attributes

Sequence length440 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) By similarity.

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

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.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

pyruvate metabolic process

Inferred from electronic annotation. Source: InterPro

   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 – 440440Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162296

Regions

Domain1 – 7777Lipoyl-binding

Sites

Active site4121 Potential

Amino acid modifications

Modified residue431N6-lipoyllysine Potential

Experimental info

Sequence conflict1691N → S in CAA63808. Ref.1
Sequence conflict186 – 1883IAE → VTG in CAA63808. Ref.1
Sequence conflict2031A → V in CAA63808. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O66119 [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: 6BC8A592FC0AF6B3

FASTA44046,833
        10         20         30         40         50         60 
MSIEVKMPAL SPTMTEGTLA KWLVKEGDAV KAGDILAEIE TDKAIMEFET VDAGIIAKIL 

        70         80         90        100        110        120 
VPEGSENIAV GQVIAVMAEA GEDVSQVAAS ASSQISEPSE KADVAQKETA DSETISIDAS 

       130        140        150        160        170        180 
LDKAISNAGY GNKTENMTAS YQEKAGRIKA SPLAKRLAKK NHVDLKQVNG SGPHGRIIKA 

       190        200        210        220        230        240 
DIEAFIAEAN QASSNPSVST PEASGKITHD TPHNSIKLSN MRRVIARRLT ESKQNIPHIY 

       250        260        270        280        290        300 
LTVDVQMDAL LKLRSELNES LAVQNIKISV NDMLIKAQAL ALKATPNVNV AFDGDQMLQF 

       310        320        330        340        350        360 
SQADISVAVS VEGGLITPIL KQADTKSLSA LSVEMKELIA RAREGRLQPQ EYQGGTSSIS 

       370        380        390        400        410        420 
NMGMFGIKQF NAVINPPQAS ILAIGSGERR PWVIDDAITI ATVATITGSF DHRVIDGADA 

       430        440 
AAFMSAFKHL VEKPLGILAQ

« Hide

References

« Hide 'large scale' references
[1]"Purification of the pyruvate dehydrogenase multienzyme complex of Zymomonas mobilis and identification and sequence analysis of the corresponding genes."
Neveling U., Klasen R., Bringer-Meyer S., Sahm H.
J. Bacteriol. 180:1540-1548(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29191 / DSM 3580 / NBRC 13756 / NCIMB 11199 / NRRL B-4490 / ZM6.
[2]"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4."
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. expand/collapse author list , Kang H.L., Lee S.Y., Lee K.J., Kang H.S.
Nat. Biotechnol. 23:63-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31821 / ZM4 / CP4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X93605 Genomic DNA. Translation: CAA63808.1.
AE008692 Genomic DNA. Translation: AAV89134.1.
RefSeqYP_162245.1. NC_006526.2.

3D structure databases

ProteinModelPortalO66119.
ModBaseSearch...

Protein-protein interaction databases

STRING264203.ZMO0510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV89134; AAV89134; ZMO0510.
GeneID3189399.
KEGGzmo:ZMO0510.
PATRIC32566342. VBIZymMob102260_0481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
KOK00627.
OMAETIAPQN.
ProtClustDBCLSK2524600.

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.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. E3_bd. 1 hit.
SSF51230. Hybrid_motif. 1 hit.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_ZYMMO
AccessionPrimary (citable) accession number: O66119
Secondary accession number(s): Q5NQ71
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: May 1, 2013
This is version 92 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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