TKFC_BOVIN
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 03-AUG-2022, entry version 78.
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}.
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DR EMBL; BT021593; AAX46440.1; -; mRNA.
DR STRING; 9913.ENSBTAP00000024227; -.
DR PaxDb; Q58DK4; -.
DR PeptideAtlas; Q58DK4; -.
DR PRIDE; 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 Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF101473; SSF101473; 1.
DR TIGRFAMs; TIGR02361; dak_ATP; 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
