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G8QPQ7

- G8QPQ7_AZOSU

UniProt

G8QPQ7 - G8QPQ7_AZOSU

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Protein
Acetyltransferase component of pyruvate dehydrogenase complex
Gene
Dsui_1577
Organism
Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma suillum)
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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.UniRule annotation
Binds 2 lipoyl cofactors covalently By similarity.UniRule annotation
Binds 3 lipoyl cofactors covalently By similarity.UniRule annotation

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. glycolytic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotation, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

PyruvateImported

Enzyme and pathway databases

BioCyciAORY640081:GHAS-1577-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:Dsui_1577Imported
OrganismiAzospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma suillum)Imported
Taxonomic identifieri640081 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzospira
ProteomesiUP000005633: 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 By similarity.UniRule annotation

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

LipoylUniRule annotationSAAS annotations

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.

G8QPQ7-1 [UniParc]FASTAAdd to Basket

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MSQTIEVKVP DIGDFKDVPV IEIFVKPGDT VKVEDPLCSL ESDKATMDVP    50
SSAAGVVKEV KIKVGDKVAE GSVVVILESA ASGAAAAAPA PQAAAPAPVA 100
AAPAAPAPVA AAPAPAASGP VEVKVPDIGD FKDVPVIEVF VKVGDTVKQE 150
DALCSLESDK ATMDVPSSAA GVVKEVRVKV GDKVSEGSVV VVLEGAAGAV 200
AAVAAAPAAA APAPAAPAVI PPELDGPAPT KPFTPAPAAA PYGLALGGKV 250
HASPSVRAFA RELGVDLSKV TATGPKSRIQ AEDVKAYIKG VMSGQTVAPT 300
QVGGGGITGG GSLDLLPWPK VDFAKFGPIE AKPLSRIKKI SGANLARNWV 350
MIPAVTYHED ADITDLEAFR VQLNKENEKS GQKLTMLAFI IKACVKVLQQ 400
FPELNTSLDG DNLVYKKYYH IGFAADTPNG LVVPVLKDAD KKGVLEIAKE 450
TGELAKLARD GKLKPADMQG ATFTISSVGG IGGTAFSPIV NAPEVAILGV 500
SKSSMKPVWN GKEFVPRLIV PLSLSADHRV IDGALATRFN AELAKLLADF 550
RRVML 555
Length:555
Mass (Da):57,010
Last modified:February 22, 2012 - v1
Checksum:i37BFFFD535968CF9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003153 Genomic DNA. Translation: AEV25966.1.
RefSeqiWP_014236665.1. NC_016616.1.
YP_005027807.1. NC_016616.1.

Genome annotation databases

EnsemblBacteriaiAEV25966; AEV25966; Dsui_1577.
GeneIDi11544488.
KEGGidsu:Dsui_1577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003153 Genomic DNA. Translation: AEV25966.1 .
RefSeqi WP_014236665.1. NC_016616.1.
YP_005027807.1. NC_016616.1.

3D structure databases

ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEV25966 ; AEV25966 ; Dsui_1577 .
GeneIDi 11544488.
KEGGi dsu:Dsui_1577.

Phylogenomic databases

KOi K00627.

Enzyme and pathway databases

BioCyci AORY640081:GHAS-1577-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. "Complete Genome Sequence of the Anaerobic Perchlorate-Reducing Bacterium Azospira suillum Strain PS."
    Byrne-Bailey K.G., Coates J.D.
    J. Bacteriol. 194:2767-2768(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-33 / DSM 13638 / PS.

Entry informationi

Entry nameiG8QPQ7_AZOSU
AccessioniPrimary (citable) accession number: G8QPQ7
Entry historyi
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: September 3, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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