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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

CCNA_01803

Organism
Caulobacter crescentus (strain NA1000 / CB15N)
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 N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • (R)-lipoateUniRule annotationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: Binds 2 lipoyl cofactors covalently.UniRule annotation
  • (R)-lipoateUniRule annotationNote: 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

BioCyciCAULONA1000:CCNA_01803-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:CCNA_01803Imported
OrganismiCaulobacter crescentus (strain NA1000 / CB15N)Imported
Taxonomic identifieri565050 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
ProteomesiUP000001364: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Interactioni

Protein-protein interaction databases

STRINGi190650.CC_1729.

Structurei

3D structure databases

ProteinModelPortaliB8GW76.
SMRiB8GW76. Positions 5-68, 197-428.
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.
OMAiVESCIIT.
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.

B8GW76-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSIDILMPAL SPTMEEGTLA KWHVKVGDTV KAGDVIAEIE TDKATMEVEA
60 70 80 90 100
VDEGVVEAIL VPAGTENVKV NALIAKLAGE GDSPAPAPKV EAPKAAAAAP
110 120 130 140 150
VPAAAPAPAV PAPAAPVAAD GSRVLASPLA RRLASAAGLD LKALKGTGPH
160 170 180 190 200
GRVVKSDVEA AKSGAPAAKA APASAPAAVA PTAAAPRQIQ SLEQMGIPAG
210 220 230 240 250
SYDLVPLDGM RKTIARRMTE SFRDVPHFPL TIDLEIDALL AARAKINSLL
260 270 280 290 300
EKQGVKVSVN DIVIKAAAVA LKQVPEANAS YTPEGIAMHH HADIAVAVAV
310 320 330 340 350
DGGLITPIIR KAETKGLAQI SAEMKDLAQR AKDKKLKPEE FQGGTFSISN
360 370 380 390 400
LGMFGIKSFA SIINEPQGAI MSVGAGEQRP VVKNGEIKVA TVMTVTLTCD
410 420
HRVVDGSVGA KFLAAFRPLI EEPLTLIV
Length:428
Mass (Da):44,011
Last modified:March 3, 2009 - v1
Checksum:iA8234BA3B8D6B1B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001340 Genomic DNA. Translation: ACL95268.1.
RefSeqiWP_010919597.1. NC_011916.1.
YP_002517176.1. NC_011916.1.

Genome annotation databases

EnsemblBacteriaiACL95268; ACL95268; CCNA_01803.
GeneIDi7331269.
KEGGiccs:CCNA_01803.
PATRICi21308157. VBICauCre52860_1772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001340 Genomic DNA. Translation: ACL95268.1.
RefSeqiWP_010919597.1. NC_011916.1.
YP_002517176.1. NC_011916.1.

3D structure databases

ProteinModelPortaliB8GW76.
SMRiB8GW76. Positions 5-68, 197-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190650.CC_1729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL95268; ACL95268; CCNA_01803.
GeneIDi7331269.
KEGGiccs:CCNA_01803.
PATRICi21308157. VBICauCre52860_1772.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
KOiK00627.
OMAiVESCIIT.
OrthoDBiEOG610413.

Enzyme and pathway databases

BioCyciCAULONA1000:CCNA_01803-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "The genetic basis of laboratory adaptation in Caulobacter crescentus."
    Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
    J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NA1000 / CB15NImported.

Entry informationi

Entry nameiB8GW76_CAUCN
AccessioniPrimary (citable) accession number: B8GW76
Entry historyi
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: February 4, 2015
This is version 47 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

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 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.