ID W7MLJ1_GIBM7 Unreviewed; 579 AA.
AC W7MLJ1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:EWG48365.1};
GN ORFNames=FVEG_08163 {ECO:0000313|EMBL:EWG48365.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG48365.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG48365.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC glyceraldehyde. {ECO:0000256|ARBA:ARBA00003264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate +
CC H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216;
CC EC=2.7.1.28; Evidence={ECO:0000256|ARBA:ARBA00000031};
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:0000256|ARBA:ARBA00001015};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 2/2.
CC {ECO:0000256|ARBA:ARBA00004778}.
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000256|ARBA:ARBA00008757}.
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DR EMBL; DS022251; EWG48365.1; -; Genomic_DNA.
DR RefSeq; XP_018754556.1; XM_018896998.1.
DR AlphaFoldDB; W7MLJ1; -.
DR STRING; 334819.W7MLJ1; -.
DR EnsemblFungi; FVEG_08163T0; FVEG_08163T0; FVEG_08163.
DR GeneID; 30065920; -.
DR KEGG; fvr:FVEG_08163; -.
DR VEuPathDB; FungiDB:FVEG_08163; -.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_0_1; -.
DR OMA; ALNMNGF; -.
DR OrthoDB; 6043at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000009096; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
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 NCBIfam; TIGR02361; dak_ATP; 1.
DR PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR PANTHER; PTHR28629:SF4; TRIOKINASE_FMN CYCLASE; 1.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF82549; DAK1/DegV-like; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EWG48365.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..346
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 383..579
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 224
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 56..59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 579 AA; 60161 MW; 7F5C8E26F60B7BB7 CRC64;
MSAKHFVNDP THLVSSALHS LTLTNPSLAL DPDFKVIYRR PDSNAKAQVS IISGGGSGHE
PSFAGMVGHG MLSAAVAGTI FASPSAEQIR TAITSRVDTS KGVLVTVMNY TGDVLNFGMA
VEKAKAAGLE VKMVVVGDDV GVGRAKAGKV GRRGIAGTVL VHKISGALAA LGKPLDQVAK
YAQLTADNLV SVGASLEHVH VPGRKADTEG SLAADEVELG MGIHNEPGSG REKAELPDLV
SKMLKQLLDA ADKDRAFVSI DSKQVVLMIN NLGGVSVLEL GGITAEVASQ LESSYNIRPV
RILSGTFMTS LNGLGFSISL LNVVSPDFEA PSMIELLDAP SEVVGWSSPV QASTWEAKNT
NTRTGRAGVT GDIKSSGLKT DPGTAQAVLK KGLQKVVEAE PEVTHYDTIV GDGDCGIGLK
RGAEAILKHI DEQPLTGDVV VDLSSIVTIV ETAMDGTSGA LYAIFLNALV HALRELSPGN
ASSEVWGKAL KMSSDALAKY TPARPGDRTL VDALYPFVEA LNQTGDVKKA AEAALEGANK
TKGMQASLGR TVYIGGSGYQ EVPDPGAWGL ASFFLGLSS
//
