Q59695 (ACOC_PSEPU) 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

Gene names

Name:

acoC

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas putida group

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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.
Sequence similarities	Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Acetoin catabolism
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
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
	Chain	1 – 370	370	Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system		PRO_0000162305
Regions
	Domain	1 – 78	78	Lipoyl-binding
Amino acid modifications
	Modified residue	45	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59695 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F3DFA23B14983B9F	FASTA	370	39,638
	10 20 30 40 50 60 MSQIHTLTMP KWGLSMTEGR VDAWLKQEGD EINKGDEVLD VETDKISSSV EAPFSGVLRR 70 80 90 100 110 120 QVAKPDETLP VGALLAVVVE GEAEESEIDA VVQRFQAEFV AEGGADQAQG PAPQKAEVGG 130 140 150 160 170 180 RLLRWFELGG EGGTPLVLVH GFGGDLNNWL FNHPALAAER RVIALDLPGH GESAKALQRG 190 200 210 220 230 240 DLDELSETVL ALLDHLDIAK AHLAGHSMGG AVSLNVAGLA PQRVASLSLI ASAGLGEAIN 250 260 270 280 290 300 GQYLQGFVAA ANRNALKPQM VQLFADPALV TRQMLEDMLK FKRLEGVDEA LRQLALAIAD 310 320 330 340 350 360 GDRQRHDLRS VLGQHPALVV WGGKDAIIPA SHARKGPEAE VLVLPEAGHM VQMEAAEQVN 370 QQMLAFLRKH

References

[1]	"Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway." Huang M., Oppermann F.B., Steinbuchel A. FEMS Microbiol. Lett. 124:141-150(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L35343 Genomic DNA. Translation: AAB58981.1.
3D structure databases
ProteinModelPortal	Q59695.
ModBase	Search...
Protein family/group databases
MEROPS	S33.010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
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	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_PSEPU

Accession

Primary (citable) accession number: Q59695

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program