ID A0A0G2FK80_9PEZI Unreviewed; 434 AA.
AC A0A0G2FK80;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative dihydroxyacetone kinase {ECO:0000313|EMBL:KKY34787.1};
GN ORFNames=UCDDA912_g05244 {ECO:0000313|EMBL:KKY34787.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY34787.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY34787.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34787.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY34787.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34787.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY34787.1}.
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DR EMBL; LCUC01000186; KKY34787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2FK80; -.
DR STRING; 1214573.A0A0G2FK80; -.
DR OrthoDB; 6043at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000034680; 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; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
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:KKY34787.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..190
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 228..426
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 434 AA; 46426 MW; 035ACBD49A79433C CRC64;
MKITGAAAAR KYDFERTVNL GRSVNSQVVS IGSALDHCHV PGRQGNEAIP KDVAIVGAGI
HNEPGAQRLS PFPPVEELIQ YCLKLLCDPE DQERYFVTFE KGDSTVLVMN NYGGLSNLEL
GALTDETITQ LASKWDIKPV RVLTGTFETS LNAPGFSISL CNLSAASRDS DTSVNELLEL
LDAPTTAVGW PNLTAPKSHL SGAKQQQNFQ TKGKIKSNNS ADITLDAKQL DTVIRSACEA
AIAAEPNLTK WDTIMGDGDC GEAVKGVSES VINILNMNGA GKGSVLDFLD ATMDAVDNMG
GTLGAILGIL LSAFASALKE QSTNPSSRIS EQFATALEQA VAALKTHTSA REGDRTVMDV
LLPFADEFAQ SKDFHRAVGV AKERAEATKF LKARFGRATY IAEAQGQELP DPGAWALYEW
LGGMSRAIKT FQVN
//
