DHAM_PROSM
ID DHAM_PROSM Reviewed; 477 AA.
AC P0DN88; A0A140NLU6;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 26.
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};
GN OrderedLocusNames=S70_05330 {ECO:0000312|EMBL:AFH92942.1};
OS Providencia stuartii (strain MRSN 2154).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1157951;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154;
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete genome sequence of Providencia stuartii clinical isolate MRSN
RT 2154.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN-LYSINE DEACETYLASE ACTIVITY, AND CAUTION.
RC STRAIN=MRSN 2154;
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-435 -> His-170 -> 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}.
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DR EMBL; CP003488; AFH92942.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DN88; -.
DR SMR; P0DN88; -.
DR EnsemblBacteria; AFH92942; AFH92942; S70_05330.
DR KEGG; psi:S70_05330; -.
DR PATRIC; fig|1157951.4.peg.1055; -.
DR HOGENOM; CLU_045361_0_0_6; -.
DR OMA; TDHVLVM; -.
DR Proteomes; UP000005012; 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: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; 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; IPR036618; PtsI_HPr-bd_sf.
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 PRINTS; PR00107; PHOSPHOCPHPR.
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.
PE 3: Inferred from homology;
KW Transferase.
FT CHAIN 1..477
FT /note="PEP-dependent dihydroxyacetone kinase, phosphoryl
FT donor subunit DhaM"
FT /id="PRO_0000435891"
FT DOMAIN 1..135
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT DOMAIN 156..243
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT REGION 269..477
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 170
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 435
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P37349"
SQ SEQUENCE 477 AA; 51763 MW; 92D01720412F0E97 CRC64;
MIGLIIVSHS KLLADGLHQL AAQMQNKQKC HIITAAGVDD ETHPIGTDAV KVMEAIESLS
DAEHIILLMD LGSALLSAET ALDLIDPDLA EKVHLCSAPL VEGAIAITAA ASGGASIDEI
LNEAQQALQA KQQQLNDTVT TTENEKDKHT HFSEQALTTQ WVVKNPSGLH IRPAAKLATL
LSGFTATLEL RHGEKRADAK SMNQIALLQV RQGDKITLVA EGVDSQNAIN AFNQLAQHNF
GDNIATTDSK TFVGKTAYVP TVAGLAHHHA PNTELCISSY QTSENETRRA TKAIEQLKTH
LDSLANTLNE QYGEEIANIF RGHRLLLEDD ELVESITQSI ENECNTAYDA ISNIFNNMSK
QYQQLDDEYL QARFIDIEDL KNQLLMSISS VAQPSCAFTE PTIILSGNLG PSELLRYRNT
NVVGVALANG SPYSHTCIIA AKMGLPILTD LGDNIHQIAE QTKLQLSIET RSLIVAS
