NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-28.
PubMed=2061286 [NCBI, ExPASy, EBI, Israel, Japan]
Priefert H., Hein S., Krueger N., Zeh K., Schmidt B., Steinbuechel A.;
"Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism.";
J. Bacteriol. 173:4056-4071(1991).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt1244; PubMed=16964242 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16.";
Nat. Biotechnol. 24:1257-1262(2006).

Comments

FUNCTION: Dihydrolipoamide acetyltransferase involved in acetoin catabolism.
CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(S-acetyldihydrolipoyl)lysine.
COFACTOR: Binds 1 lipoyl cofactor covalently (By similarity).
PATHWAY: Ketone degradation; acetoin degradation .
INDUCTION: By growth on acetoin.
SIMILARITY: Contains 1 lipoyl-binding domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M66060; AAA21950.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM260480; CAJ94952.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_728317.1; -.

3D structure databases

HSSP

O31243; 1EHY. [HSSP ENTRY / PDB]

ModBase

P27747.

Protein family/group databases

MEROPS

S33.010; -.

Ontologies

GO:0004742;	Molecular function: dihydrolipoyllysine-residue acetyltransferase activity (inferred from electronic annotation from EC).
GO:0016787;	Molecular function: hydrolase activity (inferred from electronic annotation from InterPro).
GO:0031405;	Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0045150;	Biological process: acetoin catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR003089; AB_hydrolase.
IPR000073; AB_hydrolase_1.
IPR000089; Biotin_lipoyl.
Graphical view of domain structure.

Pfam

PF00561; Abhydrolase_1; 1.
PF00364; Biotin_lipoyl; 1.
Pfam graphical view of domain structure.

PRINTS

PR00111; ABHYDROLASE.

PROSITE

PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P27747.

Genome annotation databases

GeneID

4454951; -.

GenomeReviews

AM260480_GR; H16_B0146.

KEGG

reh:H16_B0146; -.

Phylogenomic databases

HOGENOM

P27747; -.

Genome annotation databases

CMR

P27747; H16_B0146.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetoin catabolism; Acyltransferase; Complete proteome; Direct protein sequencing; Lipoyl; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 374`	`373`	`Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system.`	`PRO_0000162304`
`DOMAIN`	`10 83`	`74`	`Lipoyl-binding.`
`BINDING`	`50 50`		`Lipoyl (covalent) (By similarity).`
`CONFLICT`	`95 95`		`D -> G (in Ref. 1; AAA21950).`
`CONFLICT`	`121 121`		`V -> G (in Ref. 1; AAA21950).`

Sequence information

Length: 374 AA [This is the length of the unprocessed precursor]

Molecular weight: 39135 Da [This is the MW of the unprocessed precursor]

CRC64: 0EBD42C03A81A189 [This is a checksum on the sequence]

        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

P27747 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools