DHAL2_LISIN
ID DHAL2_LISIN Reviewed; 216 AA.
AC Q92EU3;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=PEP-dependent dihydroxyacetone kinase 2, ADP-binding subunit DhaL {ECO:0000305|PubMed:22773791};
DE EC=2.7.1.121 {ECO:0000305|PubMed:22773791};
GN Name=dhaL-2 {ECO:0000303|PubMed:22773791};
GN OrderedLocusNames=lin0365 {ECO:0000312|EMBL:CAC95598.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626 {ECO:0000312|Proteomes:UP000002513};
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
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: 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:0000305|PubMed:22773791}.
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:0000305|PubMed:22773791};
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:0000305|PubMed:22773791}.
CC -!- INDUCTION: Repressed by GolR. {ECO:0000269|PubMed:22773791}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity.
CC {ECO:0000305|PubMed:22773791}.
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DR EMBL; AL596164; CAC95598.1; -; Genomic_DNA.
DR PIR; AF1478; AF1478.
DR RefSeq; WP_003770292.1; NC_003212.1.
DR AlphaFoldDB; Q92EU3; -.
DR SMR; Q92EU3; -.
DR STRING; 272626.lin0365; -.
DR EnsemblBacteria; CAC95598; CAC95598; CAC95598.
DR KEGG; lin:lin0365; -.
DR eggNOG; COG1461; Bacteria.
DR HOGENOM; CLU_066424_5_0_9; -.
DR OMA; ADQVRGC; -.
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; IDA: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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Glycerol metabolism; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Transferase.
FT CHAIN 1..216
FT /note="PEP-dependent dihydroxyacetone kinase 2, ADP-binding
FT subunit DhaL"
FT /id="PRO_0000439401"
FT DOMAIN 9..210
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 41..44
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 84..85
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 126
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 135
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P76014"
FT BINDING 182
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
FT BINDING 195..197
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:Q9CIV7"
SQ SEQUENCE 216 AA; 23125 MW; F092D7F3D5781521 CRC64;
MSELVMDSAF FGHVLQDMGA LIEKERDYLT GLDSDIGDGD HGINLSIGFR EVNKQLDELL
TVSPDIATLL KKSGMILLGK VGGASGPLYG SFFMKCGADV PGKTEVNFDE LCGMIINGAA
AVQHRGKAEL GDKTMMDAFL PGVEVLQNRD TNADPIETFS AFVDAMHAGA QSTIPLIAKK
GRALRLGERA IGHLDPGSES SWMLMNVILE NLKKAV
