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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

BG75_04065

Organism
Rickettsia endosymbiont of Proechinophthirus fluctus
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.UniRule annotation

Cofactori

(R)-lipoateUniRule annotationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferaseUniRule annotation, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
ORF Names:BG75_04065Imported
OrganismiRickettsia endosymbiont of Proechinophthirus fluctusImported
Taxonomic identifieri1462733 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsia
Proteomesi
  • UP000075796 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 78Lipoyl-bindingInterPro annotationAdd BLAST77
Domaini132 – 169Peripheral subunit-binding (PSBD)InterPro annotationAdd BLAST38

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili294 – 314Sequence analysisAdd BLAST21

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation

Keywords - Domaini

Coiled coilSequence analysis, LipoylUniRule annotationSAAS annotation

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

A0A161QP32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIKILMPAL SPTMTEGNLA RWLKKEGDKV NPGEVIAEIE TDKATMEVEA
60 70 80 90 100
VDEGILAKIV IPQNSQNVPV NSLIAVLSEE GEEKTDIDAF IAKNNSVSPS
110 120 130 140 150
PKTDANLPKP HENITNVEEQ VTVIKHDASK IFASPLAKRL AKMRNIRFES
160 170 180 190 200
VKGSGPHGRI VKQDILSYTP STAHNKIVIR NPEEYRLVPN NNIHKIIAKR
210 220 230 240 250
LLESKQTVPH FYLSIECNVD QLLDIREDIN KSFSEDKSTR ISVNDFIILA
260 270 280 290 300
VAKALQEVPN ANASWGEDAI RYYNNIDISV AVAIENGLVT PIVKNANQKN
310 320 330 340 350
ILELSREMKA LIKKAKDNKL TPEEFQGGGF TISNLGMYGI KNFNAIINPP
360 370 380 390 400
QSCIMGVGAI AKRAIVKNDQ ITIATIMDVT LSADHRVVDG AVGAEFLTAF
410
KKFIESPVLM LI
Length:412
Mass (Da):45,389
Last modified:July 6, 2016 - v1
Checksum:i452AE84BF802F278
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LECS01000004 Genomic DNA Translation: KYP98167.1
RefSeqiWP_062811531.1, NZ_LECS01000004.1

Genome annotation databases

EnsemblBacteriaiKYP98167; KYP98167; BG75_04065
PATRICifig|1462733.3.peg.988

Entry informationi

Entry nameiA0A161QP32_9RICK
AccessioniPrimary (citable) accession number: A0A161QP32
Entry historyiIntegrated into UniProtKB/TrEMBL: July 6, 2016
Last sequence update: July 6, 2016
Last modified: March 28, 2018
This is version 11 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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