ID A0A1X2GQ65_9FUNG Unreviewed; 582 AA.
AC A0A1X2GQ65;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dak1-domain-containing protein {ECO:0000313|EMBL:ORX58935.1};
GN ORFNames=DM01DRAFT_1318453 {ECO:0000313|EMBL:ORX58935.1};
OS Hesseltinella vesiculosa.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Hesseltinella.
OX NCBI_TaxID=101127 {ECO:0000313|EMBL:ORX58935.1, ECO:0000313|Proteomes:UP000242146};
RN [1] {ECO:0000313|EMBL:ORX58935.1, ECO:0000313|Proteomes:UP000242146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3301 {ECO:0000313|EMBL:ORX58935.1,
RC ECO:0000313|Proteomes:UP000242146};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORX58935.1}.
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DR EMBL; MCGT01000006; ORX58935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2GQ65; -.
DR STRING; 101127.A0A1X2GQ65; -.
DR OrthoDB; 6043at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000242146; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242146};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..342
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 379..576
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 582 AA; 61652 MW; B404FA5C95A01E86 CRC64;
MTKPQGKHFM NASATIVQDS LQGLCYARPH LKLLADKRVV YAANVDQVAK AQVTLISGGG
SGHEGAFAGF VGDGLLTAAV CGGVFASPSA SQVLAALERV QSPNGVLVVV MNYTGDCLHF
GLAVERAKAK GIRAKLLVVK DDLASRNTRV GSRGMAATAM VIKICGAMAA QGASLDELVH
VGQEIMNHSA TLGVALDHCH VPGSSSHVTL APGEMELGMG IHNEAGIQKL PWMPAKNLVD
LMVDRLLCPE TSNLVAPEDK VTKVVLMVNN YGGTPLLEFN VIIKEAVEAI HRIPRLQLER
VLPGCFVTSL NMPGFSLSLL TIPDDKDAWL DDLDSPVQVS GWPRLPSFGS MAILGTQPTF
CLTPLMASQD QASVSGTHDV LEKVLRTILT QLKAIEPTVT SYDTVLGDGD LGASLLQAAD
AIEKNMAKIT QKANVSDALL SLADIIDHHV GGTASAIYCI YLNALANALA EQPEQSAVTS
WMDACASALT TLEKYTQARV GDRTMMDTLI PFVTTWQKTK SFENAVTAAQ QGMFATIKQK
PALGRTAYLS EDTVLKANMP DAGAFALSSI LDAIHSSLGL DE
//
