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Protein

Protein-lysine deacetylase

Gene

dhaM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Protein deacetylase that removes acetyl groups on specific lysine residues in target proteins. Regulates transcription by catalyzing deacetylation of 'Lys-52' and 'Lys-62' of the transcriptional repressor RutR. Is also able to deacetylate NhoA and RluC in vitro. Targets a distinct set of substrates compared to CobB.1 Publication
Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.1 Publication

Miscellaneous

Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKLM has no transport activity.1 Publication

Cofactori

Note: Does not use NAD+ or Zn2+ like other established KDACs.1 Publication

Kineticsi

  1. KM=2.13 µM for acetylated RutR1 Publication
  1. Vmax=0.29 µmol/min/mg enzyme for the deacetylation of RutR1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei9Tele-phosphohistidine intermediatePROSITE-ProRule annotation1 Publication1
Active sitei169Pros-phosphohistidine intermediatePROSITE-ProRule annotation1 Publication1
Active sitei200Nucleophile; for deacetylase activity1 Publication1
Active sitei430Tele-phosphohistidine intermediate1 Publication1

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • peptidyl-lysine deacetylation Source: EcoCyc
  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: InterPro

Keywordsi

Molecular functionHydrolase

Enzyme and pathway databases

BioCyciEcoCyc:EG12399-MONOMER
MetaCyc:EG12399-MONOMER
BRENDAi2.7.1.29 2026

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-lysine deacetylase1 Publication (EC:3.5.1.-1 Publication)
Alternative name(s):
Dihydroxyacetone kinase subunit M1 Publication
Lysine deacetylase1 Publication
Short name:
KDAC1 Publication
PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM1 Publication
Gene namesi
Name:dhaM1 Publication
Synonyms:ycgC
Ordered Locus Names:b1198, JW5185
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12399 dhaM

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • integral component of membrane Source: InterPro

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9H → A: Loss of phosphotransfer activity. 1 Publication1
Mutagenesisi169H → A: Loss of phosphotransfer activity. 1 Publication1
Mutagenesisi200S → A: Loss of lysine deacetylase activity. 1 Publication1
Mutagenesisi430H → A: Loss of phosphotransfer activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001867131 – 472Protein-lysine deacetylaseAdd BLAST472

Proteomic databases

PaxDbiP37349
PRIDEiP37349

2D gel databases

SWISS-2DPAGEiP37349

Interactioni

Subunit structurei

Homodimer (PubMed:11350937). The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL.1 Publication

Protein-protein interaction databases

BioGridi4260761, 22 interactors
DIPiDIP-11551N
IntActiP37349, 7 interactors
STRINGi316385.ECDH10B_1251

Structurei

3D structure databases

ProteinModelPortaliP37349
SMRiP37349
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 135PTS EIIA type-4PROSITE-ProRule annotation1 PublicationAdd BLAST135
Domaini155 – 242HPrPROSITE-ProRule annotation1 PublicationAdd BLAST88

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni264 – 472PTS EI-like, N-terminal part1 PublicationAdd BLAST209

Domaini

Consists of three domains. The N-terminal dimerization domain has the same fold as the IIA domain of the mannose transporter of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS). The middle domain is similar to HPr and the C-terminus is similar to the N-terminal domain of enzyme I (EI) of the PTS. The IIA domain of DhaM (via phospho-His-9), instead of ATP, is the phosphoryl donor to dihydroxyacetone (Dha). The phosphoryl flow likely involves HPr ('His-15') -> DhaM (His-430 -> His-169 -> His-9) -> DhaL-ADP -> Dha. The HPr-like domain of DhaM cannot efficiently substitute for the general carrier protein HPr.1 Publication

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105VDH Bacteria
COG1080 LUCA
COG1925 LUCA
COG3412 LUCA
HOGENOMiHOG000119746
KOiK05881
OMAiTDHVLVM
PhylomeDBiP37349

Family and domain databases

CDDicd00367 PTS-HPr_like, 1 hit
Gene3Di1.10.274.10, 1 hit
3.30.1340.10, 1 hit
3.40.50.510, 1 hit
InterProiView protein in InterPro
IPR012844 DhaM_N
IPR000032 HPr-like
IPR035895 HPr-like_sf
IPR008279 PEP-util_enz_mobile_dom
IPR036637 Phosphohistidine_dom_sf
IPR004701 PTS_EIIA_man-typ
IPR036662 PTS_EIIA_man-typ_sf
IPR008731 PTS_EIN
IPR001020 PTS_HPr_His_P_site
IPR036618 PtsI_HPr-bd_sf
PfamiView protein in Pfam
PF03610 EIIA-man, 1 hit
PF05524 PEP-utilisers_N, 1 hit
PF00391 PEP-utilizers, 1 hit
PF00381 PTS-HPr, 1 hit
PRINTSiPR00107 PHOSPHOCPHPR
SUPFAMiSSF47831 SSF47831, 1 hit
SSF52009 SSF52009, 1 hit
SSF53062 SSF53062, 1 hit
SSF55594 SSF55594, 1 hit
TIGRFAMsiTIGR02364 dha_pts, 1 hit
TIGR01003 PTS_HPr_family, 1 hit
PROSITEiView protein in PROSITE
PS51096 PTS_EIIA_TYPE_4, 1 hit
PS51350 PTS_HPR_DOM, 1 hit
PS00369 PTS_HPR_HIS, 1 hit

Sequencei

Sequence statusi: Complete.

P37349-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNLVIVSHS SRLGEGVGEL ARQMLMSDSC KIAIAAGIDD PQNPIGTDAV
60 70 80 90 100
KVMEAIESVA DADHVLVMMD MGSALLSAET ALELLAPEIA AKVRLCAAPL
110 120 130 140 150
VEGTLAATVS AASGADIDKV IFDAMHALEA KREQLGLPSS DTEISDTCPA
160 170 180 190 200
YDEEARSLAV VIKNRNGLHV RPASRLVYTL STFNADMLLE KNGKCVTPES
210 220 230 240 250
INQIALLQVR YNDTLRLIAK GPEAEEALIA FRQLAEDNFG ETEEVAPPTL
260 270 280 290 300
RPVPPVSGKA FYYQPVLCTV QAKSTLTVEE EQDRLRQAID FTLLDLMTLT
310 320 330 340 350
AKAEASGLDD IAAIFSGHHT LLDDPELLAA ASELLQHEHC TAEYAWQQVL
360 370 380 390 400
KELSQQYQQL DDEYLQARYI DVDDLLHRTL VHLTQTKEEL PQFNSPTILL
410 420 430 440 450
AENIYPSTVL QLDPAVVKGI CLSAGSPVSH SALIARELGI GWICQQGEKL
460 470
YAIQPEETLT LDVKTQRFNR QG
Length:472
Mass (Da):51,449
Last modified:November 24, 2009 - v3
Checksum:i7CEBEFBA1544C65E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC74282.4
AP009048 Genomic DNA Translation: BAA36055.1
X15868 Genomic DNA No translation available.
PIRiC64866
RefSeqiNP_415716.4, NC_000913.3
WP_001301101.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74282; AAC74282; b1198
BAA36055; BAA36055; BAA36055
GeneIDi945749
KEGGiecj:JW5185
eco:b1198
PATRICifig|1411691.4.peg.1087

Similar proteinsi

Entry informationi

Entry nameiDHAM_ECOLI
AccessioniPrimary (citable) accession number: P37349
Secondary accession number(s): P76013
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 24, 2009
Last modified: March 28, 2018
This is version 158 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

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