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Q7WAB6

- Q7WAB6_BORPA

UniProt

Q7WAB6 - Q7WAB6_BORPA

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Status
Unreviewed - 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:
  • Note: Binds 1 lipoyl cofactor covalently.UniRule annotation
  • Note: Binds 2 lipoyl cofactors covalently.UniRule annotation
  • Note: 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 annotationImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

PyruvateImported

Enzyme and pathway databases

BioCyciBPAR257311:BPP1463-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Name:aceFImported
Ordered Locus Names:BPP1463Imported
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)Imported
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001421: 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

Protein-protein interaction databases

STRINGi257311.BPP1463.

Structurei

3D structure databases

ProteinModelPortaliQ7WAB6.
SMRiQ7WAB6. Positions 4-83, 116-193, 302-540.
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

HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.

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.

Q7WAB6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNIVEIKVP DIGDFKEVEV IEVLVSAGDT IKAEQSLITV ESDKASMEIP
60 70 80 90 100
ASAAGVVKSV KVKVGDKIAE GTVILEVEAA GEAAAAPKAE QAPEAAEAPK
110 120 130 140 150
ADAAKAEAPA AAGPIEVKVP DIGDFKEVEV IEVLVAEGDT IKAEQSLITV
160 170 180 190 200
ESDKASMEIP ASAGGVVQSL KVKVGDKVAM GTVIAVVQGQ GAAAPAAKAE
210 220 230 240 250
APAAAEPAAS ASASAPAPAQ RPAPAAALQD EDLKPGQLPH ASPSVRKFAR
260 270 280 290 300
ELGVNLSRVT GSAAKGRITA DDVRAYVKQA LSAGAPAGAS GGGDGAALGL
310 320 330 340 350
LPWPKIDFTK FGPIEAKPLS RIKKISGANL HRNWVMIPHV TNNDEADITD
360 370 380 390 400
LEALRVALNK ENEKSGVKVT MLAFLIKAVV AALKKFPEFN ASLDGDNLVL
410 420 430 440 450
KQYYHIGFAA DTPNGLVVPV VRDADKKGIL ELARETSELA RKAREGKVSP
460 470 480 490 500
AEMQGGCFSI SSLGGIGGTH FTPIINAPEV AILGVSRSAH KPVWDGKQFV
510 520 530 540
PRLTLPLSLS YDHRVIDGAS AARFNAYLGQ LLADFRRIAL
Length:540
Mass (Da):55,912
Last modified:October 1, 2003 - v1
Checksum:i8266657E32C4D3D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640427 Genomic DNA. Translation: CAE36765.1.
RefSeqiNP_883761.1. NC_002928.3.
WP_010928050.1. NC_002928.3.

Genome annotation databases

EnsemblBacteriaiCAE36765; CAE36765; BPP1463.
GeneIDi1665553.
KEGGibpa:BPP1463.
PATRICi21146623. VBIBorPar43418_1521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640427 Genomic DNA. Translation: CAE36765.1 .
RefSeqi NP_883761.1. NC_002928.3.
WP_010928050.1. NC_002928.3.

3D structure databases

ProteinModelPortali Q7WAB6.
SMRi Q7WAB6. Positions 4-83, 116-193, 302-540.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257311.BPP1463.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE36765 ; CAE36765 ; BPP1463 .
GeneIDi 1665553.
KEGGi bpa:BPP1463.
PATRICi 21146623. VBIBorPar43418_1521.

Phylogenomic databases

HOGENOMi HOG000281562.
KOi K00627.
OMAi TEIMVAV.

Enzyme and pathway databases

BioCyci BPAR257311:BPP1463-MONOMER.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12822 / ATCC BAA-587 / NCTC 13253Imported.

Entry informationi

Entry nameiQ7WAB6_BORPA
AccessioniPrimary (citable) accession number: Q7WAB6
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: November 26, 2014
This is version 79 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