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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

Dd703_0675

Organism
Dickeya paradisiaca (strain Ech703) (Dickeya dadantii (strain Ech703))
Status
Unreviewed-Annotation score: 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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.UniRule annotation

Cofactori

(R)-lipoateUniRule annotationNote: Binds 3 lipoyl cofactors covalently.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferaseUniRule annotationImported, Transferase
Biological processGlycolysisUniRule annotation
LigandPyruvateImported

Enzyme and pathway databases

BioCyciDDAD579405:GHJU-682-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:Dd703_0675Imported
OrganismiDickeya paradisiaca (strain Ech703) (Dickeya dadantii (strain Ech703))Imported
Taxonomic identifieri579405 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaeDickeya
Proteomesi
  • UP000002734 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry.UniRule annotation

Protein-protein interaction databases

STRINGi579405.Dd703_0675.

Structurei

3D structure databases

ProteinModelPortaliC6C9N5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 75Lipoyl-bindingInterPro annotationAdd BLAST74
Domaini91 – 164Lipoyl-bindingInterPro annotationAdd BLAST74
Domaini192 – 265Lipoyl-bindingInterPro annotationAdd BLAST74

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4107QSN. Bacteria.
COG0508. LUCA.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTMEFESF.
OrthoDBiPOG091H05OF.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiView protein in InterPro
IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
PANTHERiPTHR43178:SF4. PTHR43178:SF4. 1 hit.
PfamiView protein in Pfam
PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiView protein in PROSITE
PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.

Sequencei

Sequence statusi: Complete.

C6C9N5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIEINVPDI GADEVEVTEV LVKVGDKVEA EQSLITVEGD KASMEVPSPQ
60 70 80 90 100
AGVVKEIKIA VGDKVATGKL IMVFEAAGAP APAAAPAASA VKDVEVPDIG
110 120 130 140 150
GDEVEVTEVL VKVGDTVAAE QSLITVEGDK ASMEVPAPFA GTVKEIKVST
160 170 180 190 200
GSKVKTGTLI MVFEVAGAAP AVAAPAAAVS ALAAAPAVSG GAKDVNVPDI
210 220 230 240 250
GGDEVEVTEV LVKVGDTVAA EQSLITVEGD KASMEVPAPF AGTVKEIKIS
260 270 280 290 300
TGSKVKTGSL IMVFEVAGAA PAAAAAPAPV AAAPAASAPA AASAPAKADG
310 320 330 340 350
KGEFAENDAY VHATPVIRRL AREFGVNLAK VKGTGRKGRI LREDVQAYVK
360 370 380 390 400
DAVKRAESAP AAGATGGSLP GLLPWPKVDF SKFGEVEEVE LGRIQKISGA
410 420 430 440 450
NLSRNWVMIP HVTHFDKTDI TDLEAFRKQQ NAEAEKRKLD VKFTPVVFIM
460 470 480 490 500
KAVAAALEQM PRFNSSLSED AQRLTLKKYI NIGVAVDTPN GLVVPVFKDV
510 520 530 540 550
NKKGIVELSR ELTVISKKAR DGKLTAGEMQ GGCFTISSIG GLGTTHFAPI
560 570 580 590 600
VNAPEVAILG VSKSAMEPVW NGKEFVPRLM MPISLSFDHR VIDGADGARF
610
ITIINNTLSD IRRLVM
Length:616
Mass (Da):63,922
Last modified:September 1, 2009 - v1
Checksum:i5788BB7835C5A854
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001654 Genomic DNA. Translation: ACS84486.1.

Genome annotation databases

EnsemblBacteriaiACS84486; ACS84486; Dd703_0675.
KEGGidda:Dd703_0675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001654 Genomic DNA. Translation: ACS84486.1.

3D structure databases

ProteinModelPortaliC6C9N5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi579405.Dd703_0675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACS84486; ACS84486; Dd703_0675.
KEGGidda:Dd703_0675.

Phylogenomic databases

eggNOGiENOG4107QSN. Bacteria.
COG0508. LUCA.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTMEFESF.
OrthoDBiPOG091H05OF.

Enzyme and pathway databases

BioCyciDDAD579405:GHJU-682-MONOMER.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiView protein in InterPro
IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
PANTHERiPTHR43178:SF4. PTHR43178:SF4. 1 hit.
PfamiView protein in Pfam
PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiView protein in PROSITE
PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiC6C9N5_DICP7
AccessioniPrimary (citable) accession number: C6C9N5
Entry historyiIntegrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: June 7, 2017
This is version 57 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.