DHAM1_LISIN
ID DHAM1_LISIN Reviewed; 124 AA.
AC Q927E4;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=PEP-dependent dihydroxyacetone kinase 1, phosphoryl donor subunit DhaM {ECO:0000250|UniProtKB:Q92ET9};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:Q92ET9};
DE AltName: Full=PTS system EIIA component {ECO:0000250|UniProtKB:Q92ET9};
DE AltName: Full=Phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:Q92ET9};
GN Name=dhaM-1 {ECO:0000303|PubMed:22773791};
GN OrderedLocusNames=lin2845 {ECO:0000312|EMBL:CAC98071.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP NOMENCLATURE.
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=22773791; DOI=10.1128/jb.00801-12;
RA Monniot C., Zebre A.C., Ake F.M., Deutscher J., Milohanic E.;
RT "Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent
RT dihydroxyacetone kinase system connected to the pentose phosphate
RT pathway.";
RL J. Bacteriol. 194:4972-4982(2012).
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:Q92ET9}.
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:Q92ET9};
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:Q9CIV6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92ET9}.
CC -!- DOMAIN: The EIIA type-4 domain is phosphorylated by phospho-HPr on a
CC histidyl residue. Then, it transfers the phosphoryl group to the EIIB
CC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00419}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity.
CC {ECO:0000250|UniProtKB:Q92ET9}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000250|UniProtKB:Q92ET9}.
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DR EMBL; AL596173; CAC98071.1; -; Genomic_DNA.
DR PIR; AG1787; AG1787.
DR RefSeq; WP_003772863.1; NC_003212.1.
DR AlphaFoldDB; Q927E4; -.
DR SMR; Q927E4; -.
DR STRING; 272626.lin2845; -.
DR EnsemblBacteria; CAC98071; CAC98071; CAC98071.
DR GeneID; 61171103; -.
DR KEGG; lin:lin2845; -.
DR eggNOG; COG3412; Bacteria.
DR HOGENOM; CLU_045361_1_0_9; -.
DR OMA; IQMDEKP; -.
DR OrthoDB; 2041582at2; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR039643; DhaM.
DR InterPro; IPR012844; DhaM_N.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR PANTHER; PTHR38594; PTHR38594; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR TIGRFAMs; TIGR02364; dha_pts; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycerol metabolism; Kinase; Phosphotransferase system;
KW Transferase.
FT CHAIN 1..124
FT /note="PEP-dependent dihydroxyacetone kinase 1, phosphoryl
FT donor subunit DhaM"
FT /id="PRO_0000439402"
FT DOMAIN 4..124
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT ACT_SITE 12
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
SQ SEQUENCE 124 AA; 13437 MW; 93E6C4EA123E634E CRC64;
MAKPYGVVII SHSKDVAKGV HDIIKEIAPD VSITHAGGTE DGRIGTSFDT VNEAIESNEA
DKVYTFYDLG SAKMNIETVE EISEKEIILF NAPILEGAYA TAAQIQMDEK PEVIAANLKT
IEIK
