P27747 (ACOC_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	acoC
Ordered Locus Names:	H16_B0146

Organism

Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus › Cupriavidus necator

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Acetoin catabolism
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	acetoin catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 374	373	Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system		PRO_0000162304
Regions
	Domain	10 – 83	74	Lipoyl-binding
Amino acid modifications
	Modified residue	50	1	N6-lipoyllysine By similarity
Experimental info
	Sequence conflict	95	1	D → G in AAA21950. Ref.1
	Sequence conflict	121	1	V → G in AAA21950. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P27747 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0EBD42C03A81A189	FASTA	374	39,135
	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

References

	« Hide 'large scale' referencesShow '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.
RefSeq	YP_728317.1. NC_008314.1.
3D structure databases
ProteinModelPortal	P27747.
ModBase	Search...
Protein-protein interaction databases
STRING	381666.H16_B0146.
Protein family/group databases
MEROPS	S33.010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ94952; CAJ94952; H16_B0146.
GeneID	4454951.
KEGG	reh:H16_B0146.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000261089.
KO	K00627.
OMA	AYETPAD.
ProtClustDB	PRK14875.
Enzyme and pathway databases
BioCyc	CNEC381666:GJUJ-3857-MONOMER.
UniPathway	UPA00040.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR000073. AB_hydrolase_1. IPR000089. Biotin_lipoyl. IPR011053. Single_hybrid_motif. [Graphical view]
Pfam	PF00561. Abhydrolase_1. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
PRINTS	PR00111. ABHYDROLASE.
SUPFAM	SSF51230. Hybrid_motif. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACOC_CUPNH

Accession

Primary (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:	May 1, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program