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Protein

Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

Gene

acoC

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. acetoin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Acetoin catabolism

Enzyme and pathway databases

UniPathwayiUPA00040.

Protein family/group databases

MEROPSiS33.010.

Names & Taxonomyi

Protein namesi
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 namesi
Name:acoC
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving systemPRO_0000162305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Structurei

3D structure databases

ProteinModelPortaliQ59695.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 7976Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQIHTLTMP KWGLSMTEGR VDAWLKQEGD EINKGDEVLD VETDKISSSV
60 70 80 90 100
EAPFSGVLRR QVAKPDETLP VGALLAVVVE GEAEESEIDA VVQRFQAEFV
110 120 130 140 150
AEGGADQAQG PAPQKAEVGG RLLRWFELGG EGGTPLVLVH GFGGDLNNWL
160 170 180 190 200
FNHPALAAER RVIALDLPGH GESAKALQRG DLDELSETVL ALLDHLDIAK
210 220 230 240 250
AHLAGHSMGG AVSLNVAGLA PQRVASLSLI ASAGLGEAIN GQYLQGFVAA
260 270 280 290 300
ANRNALKPQM VQLFADPALV TRQMLEDMLK FKRLEGVDEA LRQLALAIAD
310 320 330 340 350
GDRQRHDLRS VLGQHPALVV WGGKDAIIPA SHARKGPEAE VLVLPEAGHM
360 370
VQMEAAEQVN QQMLAFLRKH
Length:370
Mass (Da):39,638
Last modified:November 1, 1996 - v1
Checksum:iF3DFA23B14983B9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35343 Genomic DNA. Translation: AAB58981.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35343 Genomic DNA. Translation: AAB58981.1.

3D structure databases

ProteinModelPortaliQ59695.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS33.010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00040.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiACOC_PSEPU
AccessioniPrimary (citable) accession number: Q59695
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.