TKFC_PIG
ID TKFC_PIG Reviewed; 579 AA.
AC F1RKQ4; Q9TR81;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 60.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PARTIAL PROTEIN SEQUENCE OF 231-247; 334-341 AND 373-395, CATALYTIC
RP ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=7831203; DOI=10.1080/10826069408010094;
RA Miwa I., Kito Y., Okuda J.;
RT "Purification and characterization of triokinase from porcine kidney.";
RL Prep. Biochem. 24:203-223(1994).
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 (PubMed:7831203).
CC Represses IFIH1-mediated cellular antiviral response (By similarity).
CC {ECO:0000250|UniProtKB:Q3LXA3, ECO:0000250|UniProtKB:Q4KLZ6,
CC ECO:0000269|PubMed:7831203}.
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:0000269|PubMed:7831203};
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:0000269|PubMed:7831203};
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 Evidence={ECO:0000269|PubMed:7831203};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for D-glyceraldehyde {ECO:0000269|PubMed:7831203};
CC KM=5 uM for dihydroxyacetone {ECO:0000269|PubMed:7831203};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:7831203};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:7831203};
CC -!- SUBUNIT: Homodimer (PubMed:7831203). Interacts with IFIH1 (via the CARD
CC domains), the interaction is inhibited by viral infection (By
CC similarity). {ECO:0000250|UniProtKB:Q3LXA3,
CC ECO:0000269|PubMed:7831203}.
CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level).
CC {ECO:0000269|PubMed:7831203}.
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 -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000305}.
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DR EMBL; CU462918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU896534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1RKQ4; -.
DR SMR; F1RKQ4; -.
DR STRING; 9823.ENSSSCP00000013919; -.
DR PaxDb; F1RKQ4; -.
DR PeptideAtlas; F1RKQ4; -.
DR PRIDE; F1RKQ4; -.
DR eggNOG; KOG2426; Eukaryota.
DR HOGENOM; CLU_017054_6_2_1; -.
DR InParanoid; F1RKQ4; -.
DR OrthoDB; 472175at2759; -.
DR TreeFam; TF313821; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; F1RKQ4; SS.
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 1: Evidence at protein level;
KW ATP-binding; Cobalt; Direct protein sequencing; FAD; Flavoprotein; Kinase;
KW Lyase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..579
FT /note="Triokinase/FMN cyclase"
FT /id="PRO_0000418834"
FT DOMAIN 9..336
FT /note="DhaK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00814"
FT DOMAIN 372..572
FT /note="DhaL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00813"
FT REGION 346..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 557..559
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 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KLZ6"
SQ SEQUENCE 579 AA; 59234 MW; 3645CE9542C4C2C8 CRC64;
MTSKKLVNSV AGCADDALAG LVACNPSLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
AREQARAEGI PVEMVVVGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEITNR
VSVVAKAMGT LGVSLSSCSV PGSRPTFELS ADEVELGLGI HGEAGVLRIK MATADEIVAH
MLNHMTDSSN VSHVPVQSGS SVVLMVNNLG GLSYLELGII ADAAVRFLEG RGVKIARALV
GTFMSALEMP GVSLTLLLVD EPLLKLIDAE TTAAAWPNVA KVSVTGRKRS RAAPAEPPEA
PDATAAGGAT SKQMVRVLER VCTTLLGLED QLNALDRAAG DGDCGTTHSR AARAIQGWLK
ESPPPASPAQ LLSKLSLLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTDLAA WSAAMDAGLE
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGANLLPVL TKALLENAEA AAEATKNMEA
GAGRASYISS ARLDQPDPGA VAAAAILRAI LEVLQSQGA
