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A9ISY2

- A9ISY2_BORPD

UniProt

A9ISY2 - A9ISY2_BORPD

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
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

Enzyme and pathway databases

BioCyciBPET340100:GJBO-3053-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:Bpet3018Imported
OrganismiBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)Imported
Taxonomic identifieri340100 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001225: 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

STRINGi340100.Bpet3018.

Structurei

3D structure databases

ProteinModelPortaliA9ISY2.
SMRiA9ISY2. Positions 6-83, 133-212, 324-563.
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

eggNOGiCOG0508.
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.

A9ISY2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKLVEIKVP DIGDFKEVEV IEVLVSEGDT IQAEQSLITV ESDKASMEIP
60 70 80 90 100
ASSGGVVKSV KVKVGDKVAE GKVILEVEAG EAAGADQAPA SPDKADAAAK
110 120 130 140 150
QPSSGDAPKT QGQTVEAPDV KPAADAGKGA GGIAEITVPD IGDFKEVEVI
160 170 180 190 200
EVMIAVGDTI KPEQSLITVE SDKASMEIPA SAGGVVKEVK VKVGDKVAKG
210 220 230 240 250
TAIAVVEGQG GAQAEPQKAQ APAQAQEQQP SGAASASAAA PAPAAKPAPA
260 270 280 290 300
AALEDPGLKP GQLPHASPSV RKFARELGVN LSKVKGSGPK DRITADDVRA
310 320 330 340 350
FVKQALAAPA AAAGGADGAA LGLLPWPKVD FTKFGPVEAK PLSRIKKISG
360 370 380 390 400
ANLHRNWVMI PHVTNNDEAD ITDLEALRVT LNKENEKAGI KVTMLAFLIK
410 420 430 440 450
AVVAALKKFP EFNASLDGDQ LVYKQYYHIG FAADTPNGLV VPVIRDADKK
460 470 480 490 500
GILEIAKEMG ELSKKARDGK ISPAEMQGGC FSISSLGGIG GTHFTPIINA
510 520 530 540 550
PEVAILGVSR SAHKPVWDGK QFVPRLIVPL SLSYDHRVID GAAAARFNAY
560
LGQLLADFRR IVL
Length:563
Mass (Da):58,393
Last modified:February 5, 2008 - v1
Checksum:i51178C889F4ACF4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM902716 Genomic DNA. Translation: CAP43360.1.
RefSeqiWP_012249923.1. NC_010170.1.
YP_001631628.1. NC_010170.1.

Genome annotation databases

EnsemblBacteriaiCAP43360; CAP43360; Bpet3018.
GeneIDi5817454.
KEGGibpt:Bpet3018.
PATRICi21167575. VBIBorPet31633_3041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM902716 Genomic DNA. Translation: CAP43360.1 .
RefSeqi WP_012249923.1. NC_010170.1.
YP_001631628.1. NC_010170.1.

3D structure databases

ProteinModelPortali A9ISY2.
SMRi A9ISY2. Positions 6-83, 133-212, 324-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 340100.Bpet3018.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAP43360 ; CAP43360 ; Bpet3018 .
GeneIDi 5817454.
KEGGi bpt:Bpet3018.
PATRICi 21167575. VBIBorPet31633_3041.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281562.
KOi K00627.
OMAi TEIMVAV.

Enzyme and pathway databases

BioCyci BPET340100:GJBO-3053-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448Imported.

Entry informationi

Entry nameiA9ISY2_BORPD
AccessioniPrimary (citable) accession number: A9ISY2
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3