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C6C9N5

- C6C9N5_DICDC

UniProt

C6C9N5 - C6C9N5_DICDC

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

Dd703_0675

Organism
Dickeya dadantii (strain Ech703)
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

Keywords - Ligandi

PyruvateImported

Enzyme and pathway databases

BioCyciDDAD579405:GHJU-688-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 dadantii (strain Ech703)Imported
Taxonomic identifieri579405 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya
ProteomesiUP000002734: 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

STRINGi579405.Dd703_0675.

Structurei

3D structure databases

ProteinModelPortaliC6C9N5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 3 lipoyl-binding domains.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.
OrthoDBiEOG610413.

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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

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.
RefSeqiYP_002986308.1. NC_012880.1.

Genome annotation databases

EnsemblBacteriaiACS84486; ACS84486; Dd703_0675.
GeneIDi8089082.
KEGGidda:Dd703_0675.
PATRICi21788540. VBIDicDad95084_0720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001654 Genomic DNA. Translation: ACS84486.1 .
RefSeqi YP_002986308.1. NC_012880.1.

3D structure databases

ProteinModelPortali C6C9N5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 579405.Dd703_0675.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACS84486 ; ACS84486 ; Dd703_0675 .
GeneIDi 8089082.
KEGGi dda:Dd703_0675.
PATRICi 21788540. VBIDicDad95084_0720.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281562.
KOi K00627.
OMAi TEIMVAV.
OrthoDBi EOG610413.

Enzyme and pathway databases

BioCyci DDAD579405:GHJU-688-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. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ech703Imported.

Entry informationi

Entry nameiC6C9N5_DICDC
AccessioniPrimary (citable) accession number: C6C9N5
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: November 26, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3