ID M2N9Z5_BAUPA Unreviewed; 593 AA.
AC M2N9Z5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dihydroxyacetone kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BAUCODRAFT_192470 {ECO:0000313|EMBL:EMD01014.1};
OS Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS (Baudoinia compniacensis (strain UAMH 10762)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX NCBI_TaxID=717646 {ECO:0000313|EMBL:EMD01014.1, ECO:0000313|Proteomes:UP000011761};
RN [1] {ECO:0000313|EMBL:EMD01014.1, ECO:0000313|Proteomes:UP000011761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMD01014.1,
RC ECO:0000313|Proteomes:UP000011761};
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).
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; KB445550; EMD01014.1; -; Genomic_DNA.
DR RefSeq; XP_007672198.1; XM_007674008.1.
DR AlphaFoldDB; M2N9Z5; -.
DR STRING; 717646.M2N9Z5; -.
DR GeneID; 19109585; -.
DR KEGG; bcom:BAUCODRAFT_192470; -.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_0_1; -.
DR OMA; GDKLHFG; -.
DR OrthoDB; 6043at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000011761; 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:SF1; YALI0E20691P; 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:UP000011761};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..348
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 384..589
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 219
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 54..57
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 593 AA; 63664 MW; 93D07A6B66AF4879 CRC64;
MSTKHFFPHT EGVVVQGLES LVARNKHLAL DAPNKVVYSR THRPSKVTVI SGGGSGHEPA
WSGYVGDGML AAAVNGEVFA SPSTKQVMAA ISHVPSDAGI ILCITNYTGD NLHFGLAREK
AAGMGHKVAI LRMTDDVALG RKQTENTGRR GLAANMFVLK LCGSMAENGY DFEKCMRIGE
AVNANAVTVG SSLDHCHIPG REHHRSVPED TYVLGMGIHN EPGLHEVSPM PPVEEIVADM
LKYCMDPNDK DRAFVEFKPD DIVCLLINNF GGMSNFELEA LTSVTRRVLD RDWKIQPTRV
YAQCFETSLN APGWSISLLN ITGIERQTNA SVFTLLHLLD DETKAPSWPR NGYKDMKIPK
ETAKAQANGV ADSSAQKGPQ VDPATLEAAL RKACEDAVKA EPEITKWDVQ MGDGDCGEAV
EGMCKGVLKK LDSGLCKDGA LFHILDETEG AVEEIGGTLG AIISIVLASF TSNLRLAYAK
DESNFRMDIK SASMAAGQAL KNLCGYTSAR QGSRTVMDAL IPFCETLEKD VDLKKAVEAA
EEGAKSTSGM QAKFGRASYV GEKGAEASQD APPDPGAMAA AIFLRGLLDG MQK
//
