ID A0A2A2M1I9_9BILA Unreviewed; 328 AA.
AC A0A2A2M1I9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Triokinase/FMN cyclase {ECO:0000256|ARBA:ARBA00018932};
DE EC=2.7.1.28 {ECO:0000256|ARBA:ARBA00012110};
DE EC=2.7.1.29 {ECO:0000256|ARBA:ARBA00012107};
DE EC=4.6.1.15 {ECO:0000256|ARBA:ARBA00012578};
DE AltName: Full=Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing) {ECO:0000256|ARBA:ARBA00032426};
GN ORFNames=WR25_19532 {ECO:0000313|EMBL:PAV92318.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV92318.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV92318.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV92318.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC glyceraldehyde, and the splitting of ribonucleoside diphosphate-X
CC compounds among which FAD is the best substrate. Represses IFIH1-
CC mediated cellular antiviral response. {ECO:0000256|ARBA:ARBA00045490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde + ATP = D-glyceraldehyde 3-phosphate + ADP +
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:ARBA00047974};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FAD = riboflavin cyclic-4',5'-phosphate + AMP + H(+);
CC Xref=Rhea:RHEA:13729, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:76202, ChEBI:CHEBI:456215; EC=4.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00048526};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone + ATP = dihydroxyacetone phosphate + ADP +
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:ARBA00048898};
CC -!- SUBUNIT: Homodimer. Interacts with IFIH1 (via the CARD domains), the
CC interaction is inhibited by viral infection.
CC {ECO:0000256|ARBA:ARBA00046681}.
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:PAV92318.1}.
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DR EMBL; LIAE01006240; PAV92318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2M1I9; -.
DR OrthoDB; 1724672at2759; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034012; F:FAD-AMP lyase (cyclizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:TreeGrafter.
DR FunFam; 3.30.1180.20:FF:000001; Dihydroxyacetone kinase 1; 1.
DR Gene3D; 1.25.40.340; -; 1.
DR Gene3D; 3.30.1180.20; Dihydroxyacetone kinase, domain 2; 1.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR InterPro; IPR050861; Dihydroxyacetone_Kinase.
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 Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..156
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 196..328
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 328 AA; 36450 MW; D5AB71E9CD1504C9 CRC64;
MKQLLFKPYY FAGTFGVSLY PCSLPGKGPM FRLEEDEMEV GLGIHGESGR RRESAKSARE
VATDLMKDIS ECLRLKKDEP ICVLLNNLGS VSQLEMNILA AEIIQWARNA EFVIKRFYSG
TFLTSLDGHG ISITILRVYD ENLLAYLDAP TNAPAWRPST VTEVDYTKLD LKTKEEEKQV
KETDEMKDAN PTADGNLVER MMESVCEEMK KREDELNRLD GAAGDADCGS TFASAAKAIY
NAKDKLDFAH PYRLLRQVSE IFEESVGGTS GAIYALMLST ASTEFKESVS KESCISALKQ
ANEAVQKYGG ARPGDRSMVC IDFLLHTK
//
