ID   TKFC_BOVIN              Reviewed;         578 AA.
AC   Q58DK4;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Triokinase/FMN cyclase;
DE   AltName: Full=Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing);
DE   Includes:
DE     RecName: Full=ATP-dependent dihydroxyacetone kinase;
DE              Short=DHA kinase;
DE              EC=2.7.1.28;
DE              EC=2.7.1.29;
DE     AltName: Full=Glycerone kinase;
DE     AltName: Full=Triokinase;
DE     AltName: Full=Triose kinase;
DE   Includes:
DE     RecName: Full=FAD-AMP lyase (cyclizing);
DE              EC=4.6.1.15;
DE     AltName: Full=FAD-AMP lyase (cyclic FMN forming);
DE     AltName: Full=FMN cyclase;
GN   Name=TKFC; Synonyms=DAK;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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:0000250|UniProtKB:F1RKQ4,
CC       ECO:0000250|UniProtKB:Q3LXA3, ECO:0000250|UniProtKB:Q4KLZ6}.
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;
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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FAD = AMP + H(+) + riboflavin cyclic-4',5'-phosphate;
CC         Xref=Rhea:RHEA:13729, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:76202, ChEBI:CHEBI:456215; EC=4.6.1.15;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Note=Manganese or cobalt are requested for FAD-AMP lyase activity.
CC       {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Each activity is inhibited by the substrate(s) of
CC       the other. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with IFIH1 (via the CARD
CC       domains), the interaction is inhibited by viral infection (By
CC       similarity). {ECO:0000250|UniProtKB:F1RKQ4,
CC       ECO:0000250|UniProtKB:Q3LXA3}.
CC   -!- DOMAIN: DhaK and DhaL domains have differential roles, individually
CC       DhaK is inactive and DhaL displays cyclase but not kinase activity.
CC       {ECO:0000250|UniProtKB:Q3LXA3}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT021593; AAX46440.1; -; mRNA.
DR   STRING; 9913.ENSBTAP00000069894; -.
DR   PaxDb; 9913-ENSBTAP00000024227; -.
DR   PeptideAtlas; Q58DK4; -.
DR   eggNOG; KOG2426; Eukaryota.
DR   InParanoid; Q58DK4; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR   GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   ATP-binding; Cobalt; FAD; Flavoprotein; Kinase; Lyase; Magnesium;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..578
FT                   /note="Triokinase/FMN cyclase"
FT                   /id="PRO_0000121524"
FT   DOMAIN          9..336
FT                   /note="DhaK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT   DOMAIN          372..571
FT                   /note="DhaL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT   ACT_SITE        221
FT                   /note="Tele-hemiaminal-histidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT   BINDING         56..59
FT                   /ligand="dihydroxyacetone"
FT                   /ligand_id="ChEBI:CHEBI:16016"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="dihydroxyacetone"
FT                   /ligand_id="ChEBI:CHEBI:16016"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT   BINDING         114
FT                   /ligand="dihydroxyacetone"
FT                   /ligand_id="ChEBI:CHEBI:16016"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT   BINDING         401..404
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         446..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         494..495
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         556..558
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3LXA3"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3LXA3"
FT   MOD_RES         545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KLZ6"
SQ   SEQUENCE   578 AA;  59124 MW;  04F870A1C05001E4 CRC64;
     MTSKKLVNSV AGCADDALAG LVACNPSLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
     PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
     AREQARAEGI PVEMVVVGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEITDR
     VSVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATANEIVAL
     MLDHMTSSSN ASHVPVPPGS SVVLMVNNLG GLSFLELGII ADAAVCSLEG HGVKIARALV
     GTFMSALEMP GVSLTLLLVD EPLLKLIDAE TTASAWPNVA KVWVTGRKRS RAAPTEPLAA
     PDSTTAAGEA SKQMVLVLEW VCTTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIXGWLK
     EGPPPASPAQ LLSKLSFLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTDLPA WSAAMDAGLE
     AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGANMLQIL TKAVKSAEAA AEATKNMEAG
     AGRASYISSA RLDQPDPGAV AAAAILRAIL EVLQSQGA
//