ID M2UR18_COCH5 Unreviewed; 584 AA.
AC M2UR18;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Dihydroxyacetone kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCHEDRAFT_1225829 {ECO:0000313|EMBL:EMD90332.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD90332.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD90332.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445578; EMD90332.1; -; Genomic_DNA.
DR AlphaFoldDB; M2UR18; -.
DR STRING; 701091.M2UR18; -.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_0_1; -.
DR OMA; QCDIENK; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000016936; Unassembled WGS sequence.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016936};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..344
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 381..580
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 221
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 53..56
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 584 AA; 61254 MW; 4FA69FD03A3B3309 CRC64;
MSSKHFIHDP THLVNTALLS IPKTNPSVQC DIENKIIYRK NGASQVSIVS GGGSGHEPSF
ASFVGAGLLS GAVAGTIFAS PSAEQIRRCI LHRVQKDKGV LVIVMNYTGD VLNFGMAVEK
ARAAGIEADM VVVGDDAGVG RAKGGKVGRR GIAGTVLVQK IAGALAAKGV SLKDVTRVAQ
LVADNTVSIG SSLAHVHVPG RREPEEDELK DGQVEIGMGI HNEAGSERKS TDLPGLVKTM
LSHCLDVADK DRSFSSIKAE DEVVLLINNL GGVSPLELSG ITNEVVEQLA NDFKIKPVRI
LAGTFMTSLN GLGFSISILK VADTQSLGAS MLELLDAPAE ASGWAAAISS STWARRGEAK
KDEEKVEEEE VLPSDLRINY AQAKSVLTTA LNRLIAAEPD VTKYDTIVGD GDCGIGLKRG
AEAILKMLET AKETDDLLIL VNNIIQVVEL AMDGTSGAIY AIFLNALAHG LRKNSPSSPQ
PVTPAIWAKA LDSSLKALGK YTPAKPGDRT LMDALYPFIE MLSKTEDVDK AAAAAQGGAQ
GTKGMKASLG RTVYVGGEGF QEVPDPGAHG LAELLLGLSD GLKK
//
