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Q2GCH9

- Q2GCH9_NEOSM

UniProt

Q2GCH9 - Q2GCH9_NEOSM

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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Neorickettsia sennetsu (strain Miyayama)
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. pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationImported, Transferase

Keywords - Ligandi

PyruvateImported

Enzyme and pathway databases

BioCyciNSEN222891:GHFU-956-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Name:pdhCImported
Ordered Locus Names:NSE_0953Imported
OrganismiNeorickettsia sennetsu (strain Miyayama)Imported
Taxonomic identifieri222891 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeNeorickettsia
ProteomesiUP000001942: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi222891.NSE_0953.

Structurei

3D structure databases

ProteinModelPortaliQ2GCH9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 1 lipoyl-binding domain.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiPERIMEP.
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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2GCH9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVKILMPAL SPTMKEGTLA KWLVSEGEKI EAGQVIAEIE TDKATMEFEA
60 70 80 90 100
VDEGVLGKIL IPAKTAGVKV NQPIAVLLDD GEGEKELKKF LSTIDKPTVT
110 120 130 140 150
DNKAETSDGD KIKNNPSSLP ADKQQGRVIA TPLARKIASI NGIDLSLIGS
160 170 180 190 200
GSGPDGRIVK NDLLKLLDDA PQVQMHGHCT ETSIPISPMR RVIAQRLVES
210 220 230 240 250
KQNVPHFYLS VTCYLQHLLS AKKKFYDCLE TKVTVNDFVI KACAFALDKN
260 270 280 290 300
PAMNVSWEGE FIRQNQTIDI SVAVAIPDGL ITPIVFSADK LSLSSISDEV
310 320 330 340 350
RELVDKAKAG RLQPREFQGG SFTVSNLGMY GIDEFTAIIN PPQAAILAVG
360 370 380 390 400
AARKVPTVSA DAVVVSDVVT LTLSCDHRVI DGALAARFMQ SLKKAIEDPV

IML
Length:403
Mass (Da):43,468
Last modified:March 21, 2006 - v1
Checksum:i44CBB7D9749F7C7E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000237 Genomic DNA. Translation: ABD45812.1.
RefSeqiYP_506817.1. NC_007798.1.

Genome annotation databases

EnsemblBacteriaiABD45812; ABD45812; NSE_0953.
GeneIDi3931514.
KEGGinse:NSE_0953.
PATRICi22681879. VBINeoSen119815_0849.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000237 Genomic DNA. Translation: ABD45812.1 .
RefSeqi YP_506817.1. NC_007798.1.

3D structure databases

ProteinModelPortali Q2GCH9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 222891.NSE_0953.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD45812 ; ABD45812 ; NSE_0953 .
GeneIDi 3931514.
KEGGi nse:NSE_0953.
PATRICi 22681879. VBINeoSen119815_0849.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
KOi K00627.
OMAi PERIMEP.
OrthoDBi EOG610413.

Enzyme and pathway databases

BioCyci NSEN222891:GHFU-956-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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiQ2GCH9_NEOSM
AccessioniPrimary (citable) accession number: Q2GCH9
Entry historyi
Integrated into UniProtKB/TrEMBL: March 21, 2006
Last sequence update: March 21, 2006
Last modified: November 26, 2014
This is version 65 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