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Protein

Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

Gene

acoC

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

Functioni

Catalytic activityi

Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

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

Pathwayi: acetoin degradation

This protein is involved in the pathway acetoin degradation, which is part of Ketone degradation.
View all proteins of this organism that are known to be involved in the pathway acetoin degradation and in Ketone degradation.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processAcetoin catabolism

Enzyme and pathway databases

UniPathwayiUPA00040

Protein family/group databases

ESTHERipsepu-acoc AcoC_BiotinLipoyl-ABH

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001623051 – 370Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving systemAdd BLAST370

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei45N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Structurei

3D structure databases

ProteinModelPortaliQ59695
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 79Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Domaini135 – 355AB hydrolase-1Sequence analysisAdd BLAST221

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4108EMS Bacteria
COG0508 LUCA

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
IPR000089 Biotin_lipoyl
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00561 Abhydrolase_1, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PRINTSiPR00111 ABHYDROLASE
SUPFAMiSSF51230 SSF51230, 1 hit
SSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiACOC_PSEPU
AccessioniPrimary (citable) accession number: Q59695
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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