DHAK1_LISIN
ID DHAK1_LISIN Reviewed; 329 AA.
AC Q927E6;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=PTS-dependent dihydroxyacetone kinase 1, dihydroxyacetone-binding subunit DhaK {ECO:0000250|UniProtKB:Q92EU2};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:Q92EU2};
GN Name=dhaK-1 {ECO:0000303|PubMed:22773791}; OrderedLocusNames=lin2843;
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: Dihydroxyacetone binding subunit of the dihydroxyacetone
CC kinase, which is responsible for the phosphoenolpyruvate (PEP)-
CC dependent phosphorylation of dihydroxyacetone via a phosphoryl group
CC transfer from DhaL-ATP. {ECO:0000250|UniProtKB:Q92EU2}.
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:Q92EU2};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation. {ECO:0000305}.
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:Q9CIV8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92EU2}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity.
CC {ECO:0000250|UniProtKB:Q92EU2}.
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; AL596173; CAC98069.1; -; Genomic_DNA.
DR PIR; AE1787; AE1787.
DR RefSeq; WP_003772865.1; NC_003212.1.
DR AlphaFoldDB; Q927E6; -.
DR SMR; Q927E6; -.
DR STRING; 272626.lin2843; -.
DR EnsemblBacteria; CAC98069; CAC98069; CAC98069.
DR GeneID; 61171105; -.
DR KEGG; lin:lin2843; -.
DR eggNOG; COG2376; Bacteria.
DR HOGENOM; CLU_017054_0_0_9; -.
DR OMA; MLSAACP; -.
DR OrthoDB; 857242at2; -.
DR UniPathway; UPA00616; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR012736; DhaK_1.
DR InterPro; IPR004006; DhaK_dom.
DR Pfam; PF02733; Dak1; 1.
DR TIGRFAMs; TIGR02363; dhaK1; 1.
DR PROSITE; PS51481; DHAK; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycerol metabolism; Kinase; Transferase.
FT CHAIN 1..329
FT /note="PTS-dependent dihydroxyacetone kinase 1,
FT dihydroxyacetone-binding subunit DhaK"
FT /id="PRO_0000439398"
FT DOMAIN 7..329
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P76015"
FT ACT_SITE 218
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT BINDING 53..56
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV8"
FT BINDING 104
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV8"
FT BINDING 109
FT /ligand="dihydroxyacetone"
FT /ligand_id="ChEBI:CHEBI:16016"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV8,
FT ECO:0000255|PROSITE-ProRule:PRU00814"
SQ SEQUENCE 329 AA; 34899 MW; 7BF48676F8135D5E CRC64;
MKKILNGTDQ VVEQMVEGLV KSHADVVHRV EGTRVIARND KRPGKVGLVS GGGSGHEPAH
AGYVGRGMLS AAVCGDVFTS PTPDQIYEGI KAADQGAGVL LIVKNYTGDV MNFEMAADLA
DADDIKVEQI VVDDDIAVED STFTTGRRGV AGTVLVHKII GAAAEAGASL EELKALGEKV
IASVKTLGVA LSPCTVPEVG HPGFELGDDE IELGIGIHGE PGFTREKIMP SARLAKQLYE
RISSESKLLA GDKVVVLVNG MGATPLMEQY VFANDVHELL KNAGVQVEKT LVGDYMTSLE
MAGLSLTILK LEDEKWVDML KLPVDTIAW
