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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.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 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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliG8QPQ7.
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.

G8QPQ7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQTIEVKVP DIGDFKDVPV IEIFVKPGDT VKVEDPLCSL ESDKATMDVP
60 70 80 90 100
SSAAGVVKEV KIKVGDKVAE GSVVVILESA ASGAAAAAPA PQAAAPAPVA
110 120 130 140 150
AAPAAPAPVA AAPAPAASGP VEVKVPDIGD FKDVPVIEVF VKVGDTVKQE
160 170 180 190 200
DALCSLESDK ATMDVPSSAA GVVKEVRVKV GDKVSEGSVV VVLEGAAGAV
210 220 230 240 250
AAVAAAPAAA APAPAAPAVI PPELDGPAPT KPFTPAPAAA PYGLALGGKV
260 270 280 290 300
HASPSVRAFA RELGVDLSKV TATGPKSRIQ AEDVKAYIKG VMSGQTVAPT
310 320 330 340 350
QVGGGGITGG GSLDLLPWPK VDFAKFGPIE AKPLSRIKKI SGANLARNWV
360 370 380 390 400
MIPAVTYHED ADITDLEAFR VQLNKENEKS GQKLTMLAFI IKACVKVLQQ
410 420 430 440 450
FPELNTSLDG DNLVYKKYYH IGFAADTPNG LVVPVLKDAD KKGVLEIAKE
460 470 480 490 500
TGELAKLARD GKLKPADMQG ATFTISSVGG IGGTAFSPIV NAPEVAILGV
510 520 530 540 550
SKSSMKPVWN GKEFVPRLIV PLSLSADHRV IDGALATRFN AELAKLLADF

RRVML
Length:555
Mass (Da):57,010
Last modified:February 22, 2012 - v1
Checksum:i37BFFFD535968CF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CP003153 Genomic DNA. Translation: AEV25966.1 .
RefSeqi WP_014236665.1. NC_016616.1.
YP_005027807.1. NC_016616.1.

3D structure databases

ProteinModelPortali G8QPQ7.
ModBasei Search...
MobiDBi 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 / PSImported.

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: November 26, 2014
This is version 20 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