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P27747 (ACOC_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:acoC
Ordered Locus Names:H16_B0146
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dihydrolipoamide acetyltransferase involved in acetoin catabolism.

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently By similarity.

Pathway

Ketone degradation; acetoin degradation.

Induction

By growth on acetoin.

Sequence similarities

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   Biological processAcetoin catabolism
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processacetoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 374373Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system
PRO_0000162304

Regions

Domain10 – 8374Lipoyl-binding

Amino acid modifications

Modified residue501N6-lipoyllysine By similarity

Experimental info

Sequence conflict951D → G in AAA21950. Ref.1
Sequence conflict1211V → G in AAA21950. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P27747 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0EBD42C03A81A189

FASTA37439,135
        10         20         30         40         50         60 
MATEISPTII PIVMPKWGLS MKEGTVNAWL VDEGTEITVG LPILDVETDK IANAVEAPDA 

        70         80         90        100        110        120 
GTLRRKVAQA GDVLPVKALL GVLAPAEVSD AQIDDYVAAY ETPADDAGEE DAAAAYQFAD 

       130        140        150        160        170        180 
VDGIRVRYAR KGGGAETVLF IHGFGGDLDN WLFNLDPLAD AYTVVALDLP GHGQSSPRLA 

       190        200        210        220        230        240 
GTTLAQMAGF VARFMDETGI EAAHVVGHSM GGGVAAQLAV DAPQRVLSVA LVSPVGFGDA 

       250        260        270        280        290        300 
VNSGYTEGFV SAQSRRELKP VVELLFADAG LVSRQMLDDL LRYKRLDGVT EALTALGQGL 

       310        320        330        340        350        360 
FGGGRQSEQP GQRLANSGKR VLVVWGGQDQ IIPAAHAEAA PPGATVKVFA DAGHMSQMEK 

       370 
ANDFNALLKK HLGG 

« Hide

References

« Hide 'large scale' references
[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]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M66060 Genomic DNA. Translation: AAA21950.1.
AM260480 Genomic DNA. Translation: CAJ94952.1.
RefSeqYP_728317.1. NC_008314.1.

3D structure databases

ProteinModelPortalP27747.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_B0146.

Protein family/group databases

MEROPSS33.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ94952; CAJ94952; H16_B0146.
GeneID4454951.
KEGGreh:H16_B0146.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000261089.
KOK00627.
OMAAYETPAD.
OrthoDBEOG64FKGZ.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-3857-MONOMER.
RETL1328306-WGS:GSTH-5096-MONOMER.
RETL1328306-WGS:GSTH-5109-MONOMER.
UniPathwayUPA00040.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
PRINTSPR00111. ABHYDROLASE.
SUPFAMSSF51230. SSF51230. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACOC_CUPNH
AccessionPrimary (citable) accession number: P27747
Secondary accession number(s): Q0K4X2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways