DHAM_ECOLI
ID DHAM_ECOLI Reviewed; 472 AA.
AC P37349; P76013;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM {ECO:0000305|PubMed:11350937};
DE EC=2.7.1.121 {ECO:0000269|PubMed:11350937};
DE AltName: Full=Dihydroxyacetone kinase subunit M {ECO:0000303|PubMed:11350937};
GN Name=dhaM {ECO:0000303|PubMed:11350937}; Synonyms=ycgC;
GN OrderedLocusNames=b1198, JW5185;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 416-472.
RC STRAIN=K12;
RX PubMed=2671658; DOI=10.1007/bf02464903;
RA Gutierrez C., Ardourel M., Bremer E., Middendorf A., Boos W., Ehmann U.;
RT "Analysis and DNA sequence of the osmoregulated treA gene encoding the
RT periplasmic trehalase of Escherichia coli K12.";
RL Mol. Gen. Genet. 217:347-354(1989).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
RP FUNCTION AS A PHOSPHORYL DONOR FOR DIHYDROXYACETONE KINASE, CATALYTIC
RP ACTIVITY OF THE COMPLEX, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION,
RP SUBUNIT, MUTAGENESIS OF HIS-9; HIS-169 AND HIS-430, ACTIVE SITE, AND
RP DOMAIN.
RC STRAIN=K12;
RX PubMed=11350937; DOI=10.1093/emboj/20.10.2480;
RA Gutknecht R., Beutler R., Garcia-Alles L.F., Baumann U., Erni B.;
RT "The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein
RT instead of ATP as phosphoryl donor.";
RL EMBO J. 20:2480-2486(2001).
RN [7]
RP PROTEIN-LYSINE DEACETYLASE ACTIVITY, AND CAUTION.
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 [8]
RP LACK OF PROTEIN-LYSINE DEACETYLASE ACTIVITY, 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:0000269|PubMed:11350937}.
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:0000269|PubMed:11350937};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for dihydroxyacetone {ECO:0000269|PubMed:11350937};
CC Note=kcat is 2.8 sec(-1). Values measured with the DhaKLM complex.
CC {ECO:0000269|PubMed:11350937};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (PubMed:11350937). The dihydroxyacetone kinase
CC complex is composed of a homodimer of DhaM, a homodimer of DhaK and the
CC subunit DhaL. {ECO:0000269|PubMed:11350937}.
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-430 -> 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:0000305|PubMed:11350937}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKLM has no transport activity.
CC {ECO:0000269|PubMed:11350937}.
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 this
CC protein does not have any protein deacetylase activity; the discrepancy
CC observed seems to be due to contaminants having proteolytic activity
CC (PubMed:29939131). {ECO:0000269|PubMed:26716769,
CC ECO:0000269|PubMed:29939131}.
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DR EMBL; U00096; AAC74282.4; -; Genomic_DNA.
DR EMBL; AP009048; BAA36055.1; -; Genomic_DNA.
DR EMBL; X15868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64866; C64866.
DR RefSeq; NP_415716.4; NC_000913.3.
DR RefSeq; WP_001301101.1; NZ_SSZK01000010.1.
DR AlphaFoldDB; P37349; -.
DR SMR; P37349; -.
DR BioGRID; 4260761; 22.
DR BioGRID; 850116; 1.
DR ComplexPortal; CPX-2634; Dha Kinase.
DR DIP; DIP-11551N; -.
DR IntAct; P37349; 7.
DR STRING; 511145.b1198; -.
DR SWISS-2DPAGE; P37349; -.
DR jPOST; P37349; -.
DR PaxDb; P37349; -.
DR PRIDE; P37349; -.
DR EnsemblBacteria; AAC74282; AAC74282; b1198.
DR EnsemblBacteria; BAA36055; BAA36055; BAA36055.
DR GeneID; 945749; -.
DR KEGG; ecj:JW5185; -.
DR KEGG; eco:b1198; -.
DR PATRIC; fig|1411691.4.peg.1087; -.
DR EchoBASE; EB2299; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG3412; Bacteria.
DR OMA; TDHVLVM; -.
DR PhylomeDB; P37349; -.
DR BioCyc; EcoCyc:EG12399-MON; -.
DR BioCyc; MetaCyc:EG12399-MON; -.
DR BRENDA; 2.7.1.121; 2026.
DR BRENDA; 2.7.1.29; 2026.
DR SABIO-RK; P37349; -.
DR UniPathway; UPA00616; -.
DR PRO; PR:P37349; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:1990234; C:transferase complex; IPI:ComplexPortal.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:ComplexPortal.
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 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.
DR PROSITE; PS00369; PTS_HPR_HIS; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..472
FT /note="PEP-dependent dihydroxyacetone kinase, phosphoryl
FT donor subunit DhaM"
FT /id="PRO_0000186713"
FT DOMAIN 1..135
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT ECO:0000305|PubMed:11350937"
FT DOMAIN 155..242
FT /note="HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000305|PubMed:11350937"
FT REGION 264..472
FT /note="PTS EI-like, N-terminal part"
FT /evidence="ECO:0000305|PubMed:11350937"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT ECO:0000305|PubMed:11350937"
FT ACT_SITE 169
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT ECO:0000305|PubMed:11350937"
FT ACT_SITE 430
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000305|PubMed:11350937"
FT MUTAGEN 9
FT /note="H->A: Loss of phosphotransfer activity."
FT /evidence="ECO:0000269|PubMed:11350937"
FT MUTAGEN 169
FT /note="H->A: Loss of phosphotransfer activity."
FT /evidence="ECO:0000269|PubMed:11350937"
FT MUTAGEN 430
FT /note="H->A: Loss of phosphotransfer activity."
FT /evidence="ECO:0000269|PubMed:11350937"
SQ SEQUENCE 472 AA; 51449 MW; 7CEBEFBA1544C65E CRC64;
MVNLVIVSHS SRLGEGVGEL ARQMLMSDSC KIAIAAGIDD PQNPIGTDAV KVMEAIESVA
DADHVLVMMD MGSALLSAET ALELLAPEIA AKVRLCAAPL VEGTLAATVS AASGADIDKV
IFDAMHALEA KREQLGLPSS DTEISDTCPA YDEEARSLAV VIKNRNGLHV RPASRLVYTL
STFNADMLLE KNGKCVTPES INQIALLQVR YNDTLRLIAK GPEAEEALIA FRQLAEDNFG
ETEEVAPPTL RPVPPVSGKA FYYQPVLCTV QAKSTLTVEE EQDRLRQAID FTLLDLMTLT
AKAEASGLDD IAAIFSGHHT LLDDPELLAA ASELLQHEHC TAEYAWQQVL KELSQQYQQL
DDEYLQARYI DVDDLLHRTL VHLTQTKEEL PQFNSPTILL AENIYPSTVL QLDPAVVKGI
CLSAGSPVSH SALIARELGI GWICQQGEKL YAIQPEETLT LDVKTQRFNR QG
