DHAL1_LISIN
ID DHAL1_LISIN Reviewed; 198 AA.
AC Q927E5;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=PEP-dependent dihydroxyacetone kinase 1, ADP-binding subunit DhaL {ECO:0000303|PubMed:22773791};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:Q92EU3};
GN Name=dhaL-1 {ECO:0000303|PubMed:22773791};
GN OrderedLocusNames=lin2844 {ECO:0000312|EMBL:CAC98070.1};
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.
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: ADP-binding subunit of the dihydroxyacetone kinase, which is
CC responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation
CC of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl
CC group transfer from DhaM and transmits it to dihydroxyacetone binds to
CC DhaK. {ECO:0000250|UniProtKB:Q92EU3}.
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:Q92EU3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9CIV7};
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:Q9CIV7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92EU3}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity.
CC {ECO:0000250|UniProtKB:Q92EU3}.
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DR EMBL; AL596173; CAC98070.1; -; Genomic_DNA.
DR PIR; AF1787; AF1787.
DR RefSeq; WP_010991404.1; NC_003212.1.
DR AlphaFoldDB; Q927E5; -.
DR SMR; Q927E5; -.
DR STRING; 272626.lin2844; -.
DR EnsemblBacteria; CAC98070; CAC98070; CAC98070.
DR KEGG; lin:lin2844; -.
DR eggNOG; COG1461; Bacteria.
DR HOGENOM; CLU_066424_5_0_9; -.
DR OMA; FFRRWMT; -.
DR OrthoDB; 1689902at2; -.
DR UniPathway; UPA00616; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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 Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR012737; DhaK_L_YcgS.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; SSF101473; 1.
DR TIGRFAMs; TIGR02365; dha_L_ycgS; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycerol metabolism; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Transferase.
FT CHAIN 1..198
FT /note="PEP-dependent dihydroxyacetone kinase 1, ADP-binding
FT subunit DhaL"
FT /id="PRO_0000439400"
FT DOMAIN 6..194
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 38..41
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 79..80
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 120
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 129
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 166
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 179..181
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
SQ SEQUENCE 198 AA; 21530 MW; CE8FF857EDE7E70A CRC64;
MTYDKDWALR WLNDFGERVQ ENKQLLSDLD QAIGDGDHGI NMARGLSELK KAFTEKEPAD
LTDVFKTAGM TMVSKVGGAS GPLYGTAFLN MSKAVDSETI DAEGLTKVIE AGLEGIEKRG
KSHAGEKTMI DVWEPVVNAL HQEDLTDDVV EAALQKTKDL KATKGRASYL GERSIGHLDP
GAYSSALLFH AMLQTEVS
