DHAM_PANAM
ID DHAM_PANAM Reviewed; 473 AA.
AC D4GL26;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM {ECO:0000250|UniProtKB:P37349};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:P37349};
DE AltName: Full=Dihydroxyacetone kinase subunit M {ECO:0000250|UniProtKB:P37349};
GN Name=dhaM {ECO:0000250|UniProtKB:P37349, ECO:0000312|EMBL:ADD76072.1};
GN OrderedLocusNames=PANA_0905 {ECO:0000312|EMBL:ADD76072.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103;
RX PubMed=20348253; DOI=10.1128/jb.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
RN [2]
RP PROTEIN-LYSINE DEACETYLASE ACTIVITY, AND CAUTION.
RC STRAIN=LMG 5342;
RX PubMed=26716769; DOI=10.7554/elife.05322;
RA Tu S., Guo S.J., Chen C.S., Liu C.X., Jiang H.W., Ge F., Deng J.Y.,
RA Zhou Y.M., Czajkowsky D.M., Li Y., Qi B.R., Ahn Y.H., Cole P.A., Zhu H.,
RA Tao S.C.;
RT "YcgC represents a new protein deacetylase family in prokaryotes.";
RL Elife 4:E05322-E05322(2015).
RN [3]
RP NO PROTEIN-LYSINE DEACETYLASE ACTIVITY IN E.COLI ORTHOLOG, AND CAUTION.
RX PubMed=29939131; DOI=10.7554/elife.37798;
RA Kremer M., Kuhlmann N., Lechner M., Baldus L., Lammers M.;
RT "Comment on 'YcgC represents a new protein deacetylase family in
RT prokaryotes'.";
RL Elife 7:E37798-E37798(2018).
CC -!- FUNCTION: Component of the dihydroxyacetone kinase complex, which is
CC responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation
CC of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is
CC phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent
CC reaction, and a phosphorelay system on histidine residues finally leads
CC to phosphoryl transfer to DhaL and dihydroxyacetone.
CC {ECO:0000250|UniProtKB:P37349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone
CC phosphate + pyruvate; Xref=Rhea:RHEA:18381, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:16016, ChEBI:CHEBI:57642, ChEBI:CHEBI:58702;
CC EC=2.7.1.121; Evidence={ECO:0000250|UniProtKB:P37349};
CC -!- SUBUNIT: Homodimer. The dihydroxyacetone kinase complex is composed of
CC a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL.
CC {ECO:0000250|UniProtKB:P37349}.
CC -!- DOMAIN: Consists of three domains. The N-terminal dimerization domain
CC has the same fold as the IIA domain of the mannose transporter of the
CC bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS).
CC The middle domain is similar to HPr and the C-terminus is similar to
CC the N-terminal domain of enzyme I (EI) of the PTS. The IIA domain of
CC DhaM (via phospho-His-9), instead of ATP, is the phosphoryl donor to
CC dihydroxyacetone (Dha). The phosphoryl flow likely involves HPr ('His-
CC 15') -> DhaM (His-432 -> His-169 -> His-9) -> DhaL-ADP -> Dha. The HPr-
CC like domain of DhaM cannot efficiently substitute for the general
CC carrier protein HPr. {ECO:0000250|UniProtKB:P37349}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKLM has no transport activity.
CC {ECO:0000250|UniProtKB:P37349}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC -!- CAUTION: Was reported to be a protein deacetylase that removes acetyl
CC groups on specific lysine residues in target proteins
CC (PubMed:26716769). However, later experiments demonstrate that the
CC protein ortholog in E.coli does not have any protein deacetylase
CC activity; the discrepancy observed seems to be due to contaminants
CC having proteolytic activity (PubMed:29939131).
CC {ECO:0000269|PubMed:26716769, ECO:0000269|PubMed:29939131}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001875; ADD76072.1; -; Genomic_DNA.
DR RefSeq; WP_013024797.1; NC_013956.2.
DR AlphaFoldDB; D4GL26; -.
DR SMR; D4GL26; -.
DR STRING; 706191.PANA_0905; -.
DR EnsemblBacteria; ADD76072; ADD76072; PANA_0905.
DR KEGG; pam:PANA_0905; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG3412; Bacteria.
DR HOGENOM; CLU_045361_0_0_6; -.
DR OMA; TDHVLVM; -.
DR OrthoDB; 404807at2; -.
DR BioCyc; PANA706191:PANA_RS04670-MON; -.
DR Proteomes; UP000001702; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 1.10.274.10; -; 1.
DR Gene3D; 3.30.1340.10; -; 1.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR039643; DhaM.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR PANTHER; PTHR38594; PTHR38594; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR SUPFAM; SSF47831; SSF47831; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR SUPFAM; SSF55594; SSF55594; 1.
DR TIGRFAMs; TIGR02364; dha_pts; 1.
DR TIGRFAMs; TIGR01003; PTS_HPr_family; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..473
FT /note="PEP-dependent dihydroxyacetone kinase, phosphoryl
FT donor subunit DhaM"
FT /id="PRO_0000435890"
FT DOMAIN 1..137
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT DOMAIN 155..242
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT REGION 266..472
FT /note="PTS EI-like, N-terminal part"
FT /evidence="ECO:0000250|UniProtKB:P37349"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT ACT_SITE 169
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 432
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P37349"
SQ SEQUENCE 473 AA; 50178 MW; 234685BA66EC38A5 CRC64;
MVNLVIVSHS AMLGEGVEML ARQMLTGDNC RIAVAAGIDD PDHPIGTDPI KVMEAIEAVA
DTDHVLVMMD MGSALLSAET ALDLLDPVIA EKVRLCAAPL VEGTLAATVS AAAGADIDTV
IDVAMNALAA KQAQLGITPP AHAASLPAQA PDSDARSVTV TIRNHHGLHV RPASRLVAAL
AGMNADLVLE KQGQCVKPDS LNQIALLQVR CHDAVTLSAS GPDAERALAA FESLAAEDFG
EHPESMALKT SASTVEKVQG KAVFYPLPLA QPARHPCSDV GQEERRLQQA IVDTLNDLNA
LAALAEKKYG ASVAAIFSGH YTLLDDPDLF DAACKVIRND SCCAESAWYQ VLMELSQQYQ
HLDDAYLQAR FIDIEDILYR SLCHLKGRDI RLPTPDVPAI IVADDIFPSA VVNLNAQLVK
GICLREGSTL SHAAIIAQQA GIAFICQQGA VLDIIQPEDR LLIDPAAQRV SCA
