DHAK_CITFR
ID DHAK_CITFR Reviewed; 552 AA.
AC P45510;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Dihydroxyacetone kinase;
DE Short=DHA kinase;
DE EC=2.7.1.29;
DE AltName: Full=Glycerone kinase;
GN Name=dhaK;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK;
RX PubMed=7635824; DOI=10.1128/jb.177.15.4392-4401.1995;
RA Daniel R., Stuertz K., Gottschalk G.;
RT "Biochemical and molecular characterization of the oxidative branch of
RT glycerol utilization by Citrobacter freundii.";
RL J. Bacteriol. 177:4392-4401(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ATP; MAGNESIUM IONS;
RP LIPID AND DIHYDROXYACETONE, ACTIVE SITE, CATALYTIC ACTIVITY, SUBUNIT, AND
RP MUTAGENESIS OF ASP-380; ASP-385; ASP-387 AND THR-388.
RX PubMed=12966101; DOI=10.1074/jbc.m305942200;
RA Siebold C., Arnold I., Garcia-Alles L.F., Baumann U., Erni B.;
RT "Crystal structure of the Citrobacter freundii dihydroxyacetone kinase
RT reveals an eight-stranded alpha-helical barrel ATP-binding domain.";
RL J. Biol. Chem. 278:48236-48244(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of dihydroxyacetone.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate +
CC H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216;
CC EC=2.7.1.29; Evidence={ECO:0000269|PubMed:12966101,
CC ECO:0000269|PubMed:7635824};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7635824};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7635824};
CC Note=Divalent metal cations, Mg(2+) or Ca(2+).
CC {ECO:0000269|PubMed:7635824};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for dihydroxyacetone {ECO:0000269|PubMed:7635824};
CC KM=70 uM for ATP {ECO:0000269|PubMed:7635824};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12966101,
CC ECO:0000269|PubMed:7635824}.
CC -!- DOMAIN: The C-terminal domain consists of a eight-helix alpha barrel.
CC The eight helices form a pocket that includes a tightly bound
CC phospholipid. The cellular function of this lipid is unknown; it has no
CC significant effect on enzyme activity.
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DR EMBL; U09771; AAB48843.1; -; Genomic_DNA.
DR PDB; 1UN8; X-ray; 2.50 A; A/B=1-552.
DR PDB; 1UN9; X-ray; 3.10 A; A/B=2-552.
DR PDBsum; 1UN8; -.
DR PDBsum; 1UN9; -.
DR AlphaFoldDB; P45510; -.
DR SMR; P45510; -.
DR STRING; 1333848.CFNIH1_02650; -.
DR DrugBank; DB01775; Dihydroxyacetone.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR BioCyc; MetaCyc:MON-4504; -.
DR BRENDA; 2.7.1.29; 1398.
DR SABIO-RK; P45510; -.
DR UniPathway; UPA00617; UER00669.
DR EvolutionaryTrace; P45510; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.340; -; 1.
DR InterPro; IPR012734; DhaK_ATP.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; SSF101473; 1.
DR TIGRFAMs; TIGR02361; dak_ATP; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Direct protein sequencing;
KW Glycerol metabolism; Kinase; Lipid-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7635824"
FT CHAIN 2..552
FT /note="Dihydroxyacetone kinase"
FT /id="PRO_0000121528"
FT DOMAIN 8..327
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 356..548
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT ACT_SITE 220
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814,
FT ECO:0000269|PubMed:12966101"
FT BINDING 58..61
FT /ligand="substrate"
FT BINDING 109
FT /ligand="substrate"
FT BINDING 114
FT /ligand="substrate"
FT BINDING 385..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12966101"
FT BINDING 431..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12966101"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12966101"
FT BINDING 476..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12966101"
FT BINDING 533..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12966101"
FT MUTAGEN 380
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12966101"
FT MUTAGEN 385
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12966101"
FT MUTAGEN 387
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12966101"
FT MUTAGEN 388
FT /note="T->H: Reduced kinase activity."
FT /evidence="ECO:0000269|PubMed:12966101"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:1UN8"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1UN9"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 266..277
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 356..371
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1UN9"
FT HELIX 388..404
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 413..427
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 430..448
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 453..468
FT /evidence="ECO:0007829|PDB:1UN8"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 478..490
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 495..511
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:1UN8"
FT HELIX 534..547
FT /evidence="ECO:0007829|PDB:1UN8"
SQ SEQUENCE 552 AA; 57940 MW; 8208307ECF3F79EA CRC64;
MSQFFFNQRT HLVSDVIDGA IIASPWNNLA RLESDPAIRI VVRRDLNKNN VAVISGGGSG
HEPAHVGFIG KGMLTAAVCG DVFASPSVDA VLTAIQAVTG EAGCLLIVKN YTGDRLNFGL
AAEKARRLGY NVEMLIVGDD ISLPDNKHPR GIAGTILVHK IAGYFAERGY NLATVLREAQ
YAASNTFSLG VALSSCHLPQ ETDAAPRHHP GHAELGMGIH GEPGASVIDT QNSAQVVNLM
VDKLLAALPE TGRLAVMINN LGGVSVAEMA IITRELASSP LHSRIDWLIG PASLVTALDM
KGFSLTAIVL EESIEKALLT EVETSNWPTP VPPREITCVV SSHASARVEF QPSANALVAG
IVELVTATLS DLETHLNALD AKVGDGDTGS TFAAAAREIA SLLHRQQLPL NNLATLFALI
GERLTVVMGG SSGVLMSIFF TAAGQKLEQG ANVVEALNTG LAQMKFYGGA DEGDRTMIDA
LQPALTSLLA QPKNLQAAFD AAQAGAERTC LSSKANAGRA SYLSSESLLG NMDPGAQRLA
MVFKALAESE LG
