DHAL_LACLA
ID DHAL_LACLA Reviewed; 192 AA.
AC Q9CIV7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=PTS-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL {ECO:0000303|PubMed:18957416};
DE EC=2.7.1.121 {ECO:0000250|UniProtKB:Q92EU3};
GN Name=dhaL {ECO:0000303|PubMed:18957416}; OrderedLocusNames=LL0249;
GN ORFNames=L46694;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-192 IN COMPLEX WITH ADP AND
RP MAGNESIUM ION, FUNCTION, MUTAGENESIS OF ARG-114; ARG-161 AND TYR-164,
RP COFACTOR, INDUCTION, AND SUBUNIT.
RX PubMed=18957416; DOI=10.1074/jbc.m804893200;
RA Zurbriggen A., Jeckelmann J.M., Christen S., Bieniossek C., Baumann U.,
RA Erni B.;
RT "X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase
RT subunits and of a transient intersubunit complex.";
RL J. Biol. Chem. 283:35789-35796(2008).
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:0000269|PubMed:18957416}.
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:0000269|PubMed:18957416};
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:0000269|PubMed:18957416}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by dihydroxyacetone via the DhaQ-DhaS complex.
CC {ECO:0000305|PubMed:18957416}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity.
CC {ECO:0000305|PubMed:18957416}.
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DR EMBL; AE005176; AAK04347.1; -; Genomic_DNA.
DR PIR; A86656; A86656.
DR RefSeq; NP_266405.1; NC_002662.1.
DR RefSeq; WP_010905236.1; NC_002662.1.
DR PDB; 3CR3; X-ray; 2.10 A; A/B=2-192.
DR PDBsum; 3CR3; -.
DR AlphaFoldDB; Q9CIV7; -.
DR SMR; Q9CIV7; -.
DR STRING; 272623.L46694; -.
DR PaxDb; Q9CIV7; -.
DR EnsemblBacteria; AAK04347; AAK04347; L46694.
DR KEGG; lla:L46694; -.
DR PATRIC; fig|272623.7.peg.274; -.
DR eggNOG; COG1461; Bacteria.
DR HOGENOM; CLU_066424_5_0_9; -.
DR OMA; ADQVRGC; -.
DR UniPathway; UPA00616; -.
DR EvolutionaryTrace; Q9CIV7; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IDA: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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Glycerol metabolism; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..192
FT /note="PTS-dependent dihydroxyacetone kinase, ADP-binding
FT subunit DhaL"
FT /id="PRO_0000270535"
FT DOMAIN 5..189
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT BINDING 37..40
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT BINDING 78..79
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT BINDING 115
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT BINDING 124
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT BINDING 161
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:18957416"
FT BINDING 174..176
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:18957416,
FT ECO:0007744|PDB:3CR3"
FT MUTAGEN 114
FT /note="R->A: Reduces activity 3-fold."
FT /evidence="ECO:0000269|PubMed:18957416"
FT MUTAGEN 114
FT /note="R->E: Reduces activity 100-fold."
FT /evidence="ECO:0000269|PubMed:18957416"
FT MUTAGEN 161
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18957416"
FT MUTAGEN 164
FT /note="Y->A: Reduces activity about 20-fold."
FT /evidence="ECO:0000269|PubMed:18957416"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:3CR3"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 37..54
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:3CR3"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:3CR3"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:3CR3"
SQ SEQUENCE 192 AA; 20578 MW; 7609CBD5D97D1751 CRC64;
MLTIDTTIEW LGKFNEKIQE NKAYLSELDG PIGDGDHGAN MARGMSETMK ALEVSNFGNV
SEIFKKVAMT LMSKVGGASG PLYGSAFLAM SKTAIETLDT SELIYAGLEA IQKRGKAQVG
EKTMVDIWSA FLNDLQTDSA SKDNLEKVVK ASAGLLATKG RASYLGERSI GHIDPGTQSS
AYLFETLLEV VA
