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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

HIB_13900

Organism
Haemophilus influenzae (strain 10810)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.UniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • (R)-lipoateUniRule annotationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 2 lipoyl cofactors covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 3 lipoyl cofactors covalently.UniRule annotation

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotation, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

PyruvateImported

Enzyme and pathway databases

BioCyciHINF862964:GHI0-1442-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Ordered Locus Names:HIB_13900Imported
OrganismiHaemophilus influenzae (strain 10810)Imported
Taxonomic identifieri862964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000008964: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliE1X754.
SMRiE1X754. Positions 1-80, 108-186, 310-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 2 lipoyl-binding domains.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

Phylogenomic databases

KOiK00627.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E1X754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQIQIPDI GSDEVTVTEV MVNVGDTISV DQSIINVEGD KASMEVPAPE
60 70 80 90 100
AGVVKEILVK VGDKVSTGTP MLVLEAAGAA PAADEPTAPV ADAPTAPVVA
110 120 130 140 150
TAPTASAIVE VNVPDIGGDE VNVTEIMVAV GDTITEEQSL ITVEGDKASM
160 170 180 190 200
EVPAPFGGVV KEILVKSGDK VSTGSLIMRF EVLGAAPAES ASASTSAPQA
210 220 230 240 250
AAPATTAQAP QAAAPDTTAQ AAQSNNNVSG LSQEQVEAST GYAHATPVIR
260 270 280 290 300
RLAREFGVNL DKVKGTGRKG RIVKEDIEAY VKTAVKAYES GATAQATGNG
310 320 330 340 350
VANGAGLGLL PWPKVDFSKF GEIEEVELSR INKISGANLH RNWVIIPHVT
360 370 380 390 400
HFDKADITDL EAFRKEQNAL AEKQKLGVKI TPVVFIMKAV AKALEAYPRF
410 420 430 440 450
NSSITEDAQR LILKKYINIG VAVDTPNGLV VPVFKNVNKK GIIELSRELM
460 470 480 490 500
EVSKKAREGK LTASDMQGGC FTISSLGGIG TTHFAPIVNA PEVAILGVSK
510 520 530 540 550
SSMEPVWNGK EFAPRLILPM SLSFDHRVID GADGARFISY LGSVLADLRR

LVM
Length:553
Mass (Da):58,004
Last modified:November 30, 2010 - v1
Checksum:iE14013405502D0E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FQ312006 Genomic DNA. Translation: CBW29577.1.
RefSeqiWP_012054691.1. NC_016809.1.
YP_005179415.1. NC_016809.1.

Genome annotation databases

EnsemblBacteriaiCBW29577; CBW29577; HIB_13900.
GeneIDi11769762.
KEGGihiu:HIB_13900.
PATRICi43040215. VBIHaeInf165663_1441.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FQ312006 Genomic DNA. Translation: CBW29577.1.
RefSeqiWP_012054691.1. NC_016809.1.
YP_005179415.1. NC_016809.1.

3D structure databases

ProteinModelPortaliE1X754.
SMRiE1X754. Positions 1-80, 108-186, 310-553.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBW29577; CBW29577; HIB_13900.
GeneIDi11769762.
KEGGihiu:HIB_13900.
PATRICi43040215. VBIHaeInf165663_1441.

Phylogenomic databases

KOiK00627.

Enzyme and pathway databases

BioCyciHINF862964:GHI0-1442-MONOMER.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Haemophilus influenzae 10810."
    Crook D., Hood D., Moxon R., Bentley S.D., Aslett M., Parkhill J.
    Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 10810Imported.

Entry informationi

Entry nameiE1X754_HAEI1
AccessioniPrimary (citable) accession number: E1X754
Entry historyi
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: February 4, 2015
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.