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Protein

Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

Gene

acoC

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Dihydrolipoamide acetyltransferase involved in acetoin catabolism.

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Acetoin catabolism

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-3857-MONOMER.
RETL1328306-WGS:GSTH-5096-MONOMER.
RETL1328306-WGS:GSTH-5109-MONOMER.
UniPathwayiUPA00040.

Protein family/group databases

MEROPSiS33.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system (EC:2.3.1.12)
Alternative name(s):
Acetoin dehydrogenase E2 component
Dihydrolipoamide acetyltransferase component of acetoin cleaving system
Fast-migrating protein
Short name:
FMP
Gene namesi
Name:acoC
Ordered Locus Names:H16_B0146
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 374373Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving systemPRO_0000162304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Expressioni

Inductioni

By growth on acetoin.

Interactioni

Protein-protein interaction databases

STRINGi381666.H16_B0146.

Structurei

3D structure databases

ProteinModelPortaliP27747.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 8476Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000261089.
KOiK00627.
OMAiAHMVQME.
OrthoDBiEOG64FKGZ.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27747-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEISPTII PIVMPKWGLS MKEGTVNAWL VDEGTEITVG LPILDVETDK
60 70 80 90 100
IANAVEAPDA GTLRRKVAQA GDVLPVKALL GVLAPAEVSD AQIDDYVAAY
110 120 130 140 150
ETPADDAGEE DAAAAYQFAD VDGIRVRYAR KGGGAETVLF IHGFGGDLDN
160 170 180 190 200
WLFNLDPLAD AYTVVALDLP GHGQSSPRLA GTTLAQMAGF VARFMDETGI
210 220 230 240 250
EAAHVVGHSM GGGVAAQLAV DAPQRVLSVA LVSPVGFGDA VNSGYTEGFV
260 270 280 290 300
SAQSRRELKP VVELLFADAG LVSRQMLDDL LRYKRLDGVT EALTALGQGL
310 320 330 340 350
FGGGRQSEQP GQRLANSGKR VLVVWGGQDQ IIPAAHAEAA PPGATVKVFA
360 370
DAGHMSQMEK ANDFNALLKK HLGG
Length:374
Mass (Da):39,135
Last modified:January 23, 2007 - v3
Checksum:i0EBD42C03A81A189
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951D → G in AAA21950 (PubMed:2061286).Curated
Sequence conflicti121 – 1211V → G in AAA21950 (PubMed:2061286).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M66060 Genomic DNA. Translation: AAA21950.1.
AM260480 Genomic DNA. Translation: CAJ94952.1.
RefSeqiWP_010813530.1. NC_008314.1.
YP_728317.1. NC_008314.1.

Genome annotation databases

EnsemblBacteriaiCAJ94952; CAJ94952; H16_B0146.
GeneIDi4454951.
KEGGireh:H16_B0146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M66060 Genomic DNA. Translation: AAA21950.1.
AM260480 Genomic DNA. Translation: CAJ94952.1.
RefSeqiWP_010813530.1. NC_008314.1.
YP_728317.1. NC_008314.1.

3D structure databases

ProteinModelPortaliP27747.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi381666.H16_B0146.

Protein family/group databases

MEROPSiS33.010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ94952; CAJ94952; H16_B0146.
GeneIDi4454951.
KEGGireh:H16_B0146.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000261089.
KOiK00627.
OMAiAHMVQME.
OrthoDBiEOG64FKGZ.

Enzyme and pathway databases

UniPathwayiUPA00040.
BioCyciCNEC381666:GJUJ-3857-MONOMER.
RETL1328306-WGS:GSTH-5096-MONOMER.
RETL1328306-WGS:GSTH-5109-MONOMER.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism."
    Priefert H., Hein S., Krueger N., Zeh K., Schmidt B., Steinbuechel A.
    J. Bacteriol. 173:4056-4071(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Entry informationi

Entry nameiACOC_CUPNH
AccessioniPrimary (citable) accession number: P27747
Secondary accession number(s): Q0K4X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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.