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Q59695 (ACOC_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. 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
Gene names
Name:acoC
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceInferred 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 processAcetoin catabolism
   DomainLipoyl
   Molecular functionAcyltransferase
Transferase
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

Chain1 – 370370Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system
PRO_0000162305

Regions

Domain1 – 7878Lipoyl-binding

Amino acid modifications

Modified residue451N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59695 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F3DFA23B14983B9F

FASTA37039,638
        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 

« Hide

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

ProteinModelPortalQ59695.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS33.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00040.

Family and domain databases

InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000073. AB_hydrolase_1.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
PRINTSPR00111. ABHYDROLASE.
SUPFAMSSF51230. SSF51230. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACOC_PSEPU
AccessionPrimary (citable) accession number: Q59695
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 77 of the entry and version 1 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