DHAL_ECOLI
ID DHAL_ECOLI Reviewed; 210 AA.
AC P76014;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL {ECO:0000303|PubMed:11350937};
DE EC=2.7.1.121 {ECO:0000269|PubMed:11350937};
GN Name=dhaL {ECO:0000303|PubMed:11350937}; Synonyms=ycgS;
GN OrderedLocusNames=b1199, JW5186;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY OF THE COMPLEX, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=11350937; DOI=10.1093/emboj/20.10.2480;
RA Gutknecht R., Beutler R., Garcia-Alles L.F., Baumann U., Erni B.;
RT "The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein
RT instead of ATP as phosphoryl donor.";
RL EMBO J. 20:2480-2486(2001).
RN [6]
RP ROLE OF ADP, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15753087; DOI=10.1074/jbc.m500279200;
RA Baechler C., Fluekiger-Bruehwiler K., Schneider P., Baehler P., Erni B.;
RT "From ATP as substrate to ADP as coenzyme: functional evolution of the
RT nucleotide binding subunit of dihydroxyacetone kinases.";
RL J. Biol. Chem. 280:18321-18325(2005).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=15616579; DOI=10.1038/sj.emboj.7600517;
RA Baechler C., Schneider P., Baehler P., Lustig A., Erni B.;
RT "Escherichia coli dihydroxyacetone kinase controls gene expression by
RT binding to transcription factor DhaR.";
RL EMBO J. 24:283-293(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ADP AND MAGNESIUM
RP ION, COFACTOR, AND SUBUNIT.
RX PubMed=16647083; DOI=10.1016/j.jmb.2006.03.057;
RA Oberholzer A.E., Schneider P., Baumann U., Erni B.;
RT "Crystal structure of the nucleotide-binding subunit DhaL of the
RT Escherichia coli dihydroxyacetone kinase.";
RL J. Mol. Biol. 359:539-545(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-210 IN COMPLEX WITH ADP AND
RP MAGNESIUM ION, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=21209328; DOI=10.1073/pnas.1012596108;
RA Shi R., McDonald L., Cui Q., Matte A., Cygler M., Ekiel I.;
RT "Structural and mechanistic insight into covalent substrate binding by
RT Escherichia coli dihydroxyacetone kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1302-1307(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 2-210 IN COMPLEX WITH DHAR; ADP
RP AND MAGNESIUM, COFACTOR, INDUCTION, AND SUBUNIT.
RX PubMed=24440518; DOI=10.1016/j.str.2013.11.012;
RA Shi R., McDonald L., Cygler M., Ekiel I.;
RT "Coiled-coil helix rotation selects repressing or activating state of
RT transcriptional regulator DhaR.";
RL Structure 22:478-487(2014).
CC -!- FUNCTION: ADP-binding subunit of the dihydroxyacetone kinase, which is
CC responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation
CC of dihydroxyacetone (PubMed:11350937). DhaL-ADP is converted to DhaL-
CC ATP via a phosphoryl group transfer from DhaM and transmits it to
CC dihydroxyacetone bound to DhaK (PubMed:11350937). DhaL acts also as
CC coactivator of the transcription activator DhaR by binding to the
CC sensor domain of DhaR (PubMed:15616579). In the presence of
CC dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity
CC (PubMed:15616579). In the absence of dihydroxyacetone, DhaL-ADP is
CC converted by the PTS to DhaL-ATP, which does not bind to DhaR
CC (PubMed:15616579). {ECO:0000269|PubMed:11350937,
CC ECO:0000269|PubMed:15616579}.
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:0000269|PubMed:11350937};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16647083, ECO:0000269|PubMed:21209328,
CC ECO:0000269|PubMed:24440518};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for dihydroxyacetone {ECO:0000269|PubMed:11350937};
CC Note=kcat is 2.8 sec(-1). Values measured with the DhaKLM complex.
CC {ECO:0000269|PubMed:11350937};
CC Temperature dependence:
CC Complexation with ADP increases the thermal unfolding temperature
CC from 40 to 65 degrees Celsius. {ECO:0000269|PubMed:15753087};
CC -!- PATHWAY: Polyol metabolism; glycerol degradation. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (PubMed:16647083, PubMed:21209328, PubMed:24440518).
CC The dihydroxyacetone kinase complex is composed of a homodimer of DhaM,
CC a homodimer of DhaK and the subunit DhaL (PubMed:16647083,
CC PubMed:21209328). DhaL also forms a complex with DhaR
CC (PubMed:24440518). {ECO:0000269|PubMed:16647083,
CC ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518}.
CC -!- INTERACTION:
CC P76014; P76015: dhaK; NbExp=2; IntAct=EBI-9021529, EBI-544485;
CC P76014; P76016: dhaR; NbExp=3; IntAct=EBI-9021529, EBI-9153808;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Activated by DhaR. {ECO:0000269|PubMed:15616579,
CC ECO:0000269|PubMed:24440518}.
CC -!- MISCELLANEOUS: Unlike the carbohydrate-specific transporters of the
CC PTS, the complex DhaKML has no transport activity. {ECO:0000305}.
CC -!- MISCELLANEOUS: The tightly bound ADP participates in a double
CC displacement phosphoryl transfer reaction and thus plays the same role
CC as histidines, cysteines and aspartic acids in other phosphoprotein
CC intermediates. {ECO:0000269|PubMed:15753087}.
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DR EMBL; U00096; AAC74283.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36056.2; -; Genomic_DNA.
DR PIR; D64866; D64866.
DR RefSeq; NP_415717.1; NC_000913.3.
DR RefSeq; WP_000059411.1; NZ_SSZK01000010.1.
DR PDB; 2BTD; X-ray; 2.60 A; A=1-210.
DR PDB; 3PNL; X-ray; 2.20 A; B=2-210.
DR PDB; 4LRZ; X-ray; 2.32 A; A/B/C/D=2-210.
DR PDBsum; 2BTD; -.
DR PDBsum; 3PNL; -.
DR PDBsum; 4LRZ; -.
DR AlphaFoldDB; P76014; -.
DR SMR; P76014; -.
DR BioGRID; 4260762; 23.
DR ComplexPortal; CPX-2634; Dha Kinase.
DR DIP; DIP-11562N; -.
DR IntAct; P76014; 2.
DR STRING; 511145.b1199; -.
DR MoonProt; P76014; -.
DR jPOST; P76014; -.
DR PaxDb; P76014; -.
DR PRIDE; P76014; -.
DR EnsemblBacteria; AAC74283; AAC74283; b1199.
DR EnsemblBacteria; BAA36056; BAA36056; BAA36056.
DR GeneID; 58460442; -.
DR GeneID; 945748; -.
DR KEGG; ecj:JW5186; -.
DR KEGG; eco:b1199; -.
DR PATRIC; fig|1411691.4.peg.1086; -.
DR EchoBASE; EB3659; -.
DR eggNOG; COG1461; Bacteria.
DR HOGENOM; CLU_066424_5_0_6; -.
DR InParanoid; P76014; -.
DR OMA; FFRRWMT; -.
DR PhylomeDB; P76014; -.
DR BioCyc; EcoCyc:MON0-1261; -.
DR BioCyc; MetaCyc:MON0-1261; -.
DR BRENDA; 2.7.1.121; 2026.
DR BRENDA; 2.7.1.29; 2026.
DR SABIO-RK; P76014; -.
DR UniPathway; UPA00616; -.
DR EvolutionaryTrace; P76014; -.
DR PRO; PR:P76014; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990234; C:transferase complex; IPI:ComplexPortal.
DR GO; GO:0043531; F:ADP binding; IDA:EcoCyc.
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:0046835; P:carbohydrate phosphorylation; IDA:ComplexPortal.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006090; P:pyruvate metabolic process; IDA:ComplexPortal.
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..210
FT /note="PEP-dependent dihydroxyacetone kinase, ADP-binding
FT subunit DhaL"
FT /id="PRO_0000121530"
FT DOMAIN 6..206
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:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:24440518, ECO:0007744|PDB:2BTD,
FT ECO:0007744|PDB:4LRZ"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518,
FT ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL,
FT ECO:0007744|PDB:4LRZ"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518,
FT ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL,
FT ECO:0007744|PDB:4LRZ"
FT BINDING 38..41
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518,
FT ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL,
FT ECO:0007744|PDB:4LRZ"
FT BINDING 79..80
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518,
FT ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL,
FT ECO:0007744|PDB:4LRZ"
FT BINDING 121
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518,
FT ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL,
FT ECO:0007744|PDB:4LRZ"
FT BINDING 130
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518,
FT ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL,
FT ECO:0007744|PDB:4LRZ"
FT BINDING 178
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000305|PubMed:21209328, ECO:0007744|PDB:2BTD"
FT BINDING 191..193
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:16647083,
FT ECO:0000269|PubMed:21209328, ECO:0000269|PubMed:24440518,
FT ECO:0007744|PDB:2BTD, ECO:0007744|PDB:3PNL,
FT ECO:0007744|PDB:4LRZ"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3PNL"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4LRZ"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:3PNL"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 103..121
FT /evidence="ECO:0007829|PDB:3PNL"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:3PNL"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:3PNL"
SQ SEQUENCE 210 AA; 22632 MW; 91C668A3E792CB5F CRC64;
MSLSRTQIVN WLTRCGDIFS TESEYLTGLD REIGDADHGL NMNRGFSKVV EKLPAIADKD
IGFILKNTGM TLLSSVGGAS GPLFGTFFIR AAQATQARQS LTLEELYQMF RDGADGVISR
GKAEPGDKTM CDVWVPVVES LRQSSEQNLS VPVALEAASS IAESAAQSTI TMQARKGRAS
YLGERSIGHQ DPGATSVMFM MQMLALAAKE
