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Q59695

- ACOC_PSEPU

UniProt

Q59695 - ACOC_PSEPU

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Protein
Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system
Gene
acoC
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - 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

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 system
PRO_0000162305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451N6-lipoyllysine By similarity

Structurei

3D structure databases

ProteinModelPortaliQ59695.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7878Lipoyl-binding
Add
BLAST

Sequence similaritiesi

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

MSQIHTLTMP KWGLSMTEGR VDAWLKQEGD EINKGDEVLD VETDKISSSV    50
EAPFSGVLRR QVAKPDETLP VGALLAVVVE GEAEESEIDA VVQRFQAEFV 100
AEGGADQAQG PAPQKAEVGG RLLRWFELGG EGGTPLVLVH GFGGDLNNWL 150
FNHPALAAER RVIALDLPGH GESAKALQRG DLDELSETVL ALLDHLDIAK 200
AHLAGHSMGG AVSLNVAGLA PQRVASLSLI ASAGLGEAIN GQYLQGFVAA 250
ANRNALKPQM VQLFADPALV TRQMLEDMLK FKRLEGVDEA LRQLALAIAD 300
GDRQRHDLRS VLGQHPALVV WGGKDAIIPA SHARKGPEAE VLVLPEAGHM 350
VQMEAAEQVN QQMLAFLRKH 370
Length:370
Mass (Da):39,638
Last modified:November 1, 1996 - v1
Checksum:iF3DFA23B14983B9F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L35343 Genomic DNA. Translation: AAB58981.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L35343 Genomic DNA. Translation: AAB58981.1 .

3D structure databases

ProteinModelPortali Q59695.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S33.010.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00040 .

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000089. Biotin_lipoyl.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00364. Biotin_lipoyl. 1 hit.
[Graphical view ]
PRINTSi PR00111. ABHYDROLASE.
SUPFAMi SSF51230. SSF51230. 1 hit.
SSF53474. SSF53474. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 78 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

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