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P45118 (ODP2_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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
Gene names
Name:aceF
Ordered Locus Names:HI_1232
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length567 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 2 lipoyl cofactors 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 2 lipoyl-binding domains.

Ontologies

Keywords
   Biological processGlycolysis
   DomainLipoyl
Repeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

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

Chain1 – 567567Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000162279

Regions

Domain1 – 7474Lipoyl-binding 1
Domain109 – 18072Lipoyl-binding 2
Region247 – 567321Subunit binding, catalytic

Sites

Active site4841 Potential
Active site5401 Potential
Active site5441 Potential

Amino acid modifications

Modified residue411N6-lipoyllysine By similarity
Modified residue1471N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P45118 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 891DBCDEB388C5B0

FASTA56759,411
        10         20         30         40         50         60 
MSKQIQIPDI GSDEVTVTEV MVNVGDTISV DQSIINVEGD KASMEVPAPE AGVVKEILVK 

        70         80         90        100        110        120 
VGDKVSTGTP MLVLEAAGAA PAADEPTAPV ADAPTAPVVA TAPTASAIVE VNVPDIGGDE 

       130        140        150        160        170        180 
VNVTEIMVAV GDTITEEQSL ITVEGDKASM EVPAPFGGVV KEILVKSGDK VSTGSLIMRF 

       190        200        210        220        230        240 
EVLGAAPAES ASAPASTSAP QTAAPATTAQ APQAAAPDTT AQAPQAAAPD TTAQAAQSNN 

       250        260        270        280        290        300 
NVSGLSQEQV EASTGYAHAT PVIRRLAREF GVNLDKVKGT GRKGRIVKED IEAYVKTAVK 

       310        320        330        340        350        360 
AYESGATAQA TGNGVANGAG LGLLPWPKVD FSKFGEIEEV ELSRINKISG ANLHRNWVII 

       370        380        390        400        410        420 
PHVTHFDKAD ITDLEAFRKE QNALREKQKL GVKITPVVFI MKAVAKALEA YPRFNSSITE 

       430        440        450        460        470        480 
DAQRLILKKY INIGVAVDTP NGLVVPVFKN VNKKGIIELS RELMEVSKKA REGKLTASDM 

       490        500        510        520        530        540 
QGGCFTISSL GGIGTTHFAP IVNAPEVAIL GVSKSSMEPV WNGKEFAPRL ILPMSLSFDH 

       550        560 
RVIDGADGAR FISYLGSVLA DLRRLVM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22885.1.
PIRI64111.
RefSeqNP_439388.1. NC_000907.1.

3D structure databases

ProteinModelPortalP45118.
SMRP45118. Positions 1-80, 108-186, 324-567.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI1232.

Proteomic databases

PRIDEP45118.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22885; AAC22885; HI_1232.
GeneID949836.
KEGGhin:HI1232.
PATRIC20191143. VBIHaeInf48452_1284.

Phylogenomic databases

eggNOGCOG0508.
KOK00627.
OMATEIMVAV.
OrthoDBEOG610413.
PhylomeDBP45118.

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. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_HAEIN
AccessionPrimary (citable) accession number: P45118
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 103 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names