TKFC_HUMAN
ID TKFC_HUMAN Reviewed; 575 AA.
AC Q3LXA3; Q2L9C1; Q53EQ9; Q9BVA7; Q9H895;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Triokinase/FMN cyclase {ECO:0000312|HGNC:HGNC:24552};
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 {ECO:0000269|PubMed:32004446};
DE EC=2.7.1.29 {ECO:0000269|PubMed:32004446};
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 {ECO:0000312|HGNC:HGNC:24552};
GN Synonyms=DAK {ECO:0000312|HGNC:HGNC:24552};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, FAD-AMP LYASE ACTIVITY,
RP AND VARIANT THR-185.
RC TISSUE=Brain;
RX PubMed=16289032; DOI=10.1016/j.bbrc.2005.10.142;
RA Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C.;
RT "Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-
RT dependent dihydroxyacetone kinases.";
RL Biochem. Biophys. Res. Commun. 338:1682-1689(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-185, AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Brain;
RA Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C.;
RT "Human brain Dha kinase/FMN cyclase splice variant mRNA encoding a shorter
RT protein inactive as Dha kinase and FMN cyclase.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-185.
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-185.
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, IDENTITY OF TRIOKINASE AND DIHYDROXYACETONE
RP KINASE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=4688871;
RA Beutler E., Guinto E.;
RT "Dihydroxyacetone metabolism by human erythrocytes: demonstration of
RT triokinase activity and its characterization.";
RL Blood 41:559-568(1973).
RN [8]
RP INTERACTION WITH IFIH1.
RX PubMed=17600090; DOI=10.1073/pnas.0700544104;
RA Diao F., Li S., Tian Y., Zhang M., Xu L.G., Zhang Y., Wang R.P., Chen D.,
RA Zhai Z., Zhong B., Tien P., Shu H.B.;
RT "Negative regulation of MDA5- but not RIG-I-mediated innate antiviral
RT signaling by the dihydroxyacetone kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11706-11711(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DOMAIN, AND MUTAGENESIS OF
RP THR-112; LYS-204; HIS-221; ASP-401; ASP-403; CYS-404; SER-446 AND ASP-556.
RX PubMed=24569995; DOI=10.1074/jbc.m113.525626;
RA Rodrigues J.R., Couto A., Cabezas A., Pinto R.M., Ribeiro J.M., Canales J.,
RA Costas M.J., Cameselle J.C.;
RT "Bifunctional homodimeric triokinase/FMN cyclase: contribution of protein
RT domains to the activities of the human enzyme and molecular dynamics
RT simulation of domain movements.";
RL J. Biol. Chem. 289:10620-10636(2014).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP INVOLVEMENT IN TKFCD, FUNCTION, CATALYTIC ACTIVITY, VARIANTS TKFCD SER-445
RP AND ILE-543, AND CHARACTERIZATION OF VARIANTS TKFCD SER-445 AND ILE-543.
RX PubMed=32004446; DOI=10.1016/j.ajhg.2020.01.005;
RA Wortmann S.B., Meunier B., Mestek-Boukhibar L., van den Broek F.,
RA Maldonado E.M., Clement E., Weghuber D., Spenger J., Jaros Z., Taha F.,
RA Yue W.W., Heales S.J., Davison J.E., Mayr J.A., Rahman S.;
RT "Bi-allelic variants in TKFC encoding triokinase/FMN cyclase are associated
RT with cataracts and multisystem disease.";
RL Am. J. Hum. Genet. 106:256-263(2020).
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 (PubMed:17600090).
CC {ECO:0000250|UniProtKB:F1RKQ4, ECO:0000250|UniProtKB:Q4KLZ6,
CC ECO:0000269|PubMed:16289032, ECO:0000269|PubMed:17600090,
CC ECO:0000269|PubMed:32004446, ECO:0000269|PubMed:4688871}.
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:32004446,
CC ECO:0000269|PubMed:4688871};
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:32004446,
CC ECO:0000269|PubMed:4688871};
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:4688871};
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.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for dihydroxyacetone {ECO:0000269|PubMed:4688871};
CC KM=11 uM for glyceraldehyde {ECO:0000269|PubMed:4688871};
CC KM=1.55 uM for dihydroxyacetone {ECO:0000269|PubMed:24569995};
CC KM=43.2 uM for ATP {ECO:0000269|PubMed:24569995};
CC KM=18.1 uM for glyceraldehyde {ECO:0000269|PubMed:24569995};
CC KM=7 uM for FAD {ECO:0000269|PubMed:24569995};
CC KM=12 uM for ADP-glucose {ECO:0000269|PubMed:24569995};
CC KM=317 uM for UDP-glucose {ECO:0000269|PubMed:24569995};
CC KM=263 uM for UDP-galactose {ECO:0000269|PubMed:24569995};
CC pH dependence:
CC Optimum pH is 6.6. {ECO:0000269|PubMed:4688871};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with IFIH1 (via the CARD
CC domains), the interaction is inhibited by viral infection
CC (PubMed:17600090). {ECO:0000250|UniProtKB:F1RKQ4,
CC ECO:0000269|PubMed:17600090}.
CC -!- INTERACTION:
CC Q3LXA3; Q9BYX4: IFIH1; NbExp=5; IntAct=EBI-4291069, EBI-6115771;
CC Q3LXA3; O00560: SDCBP; NbExp=3; IntAct=EBI-4291069, EBI-727004;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3LXA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3LXA3-2; Sequence=VSP_057181;
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
CC {ECO:0000269|PubMed:4688871}.
CC -!- DOMAIN: DhaK and DhaL domains have differential roles, individually
CC DhaK is inactive and DhaL displays cyclase but not kinase activity.
CC {ECO:0000269|PubMed:24569995}.
CC -!- DISEASE: Triokinase and FMN cyclase deficiency syndrome (TKFCD)
CC [MIM:618805]: An autosomal recessive disease characterized by cataracts
CC and developmental delay that may be associated with cerebellar
CC hypoplasia. Additional features may include liver dysfunction,
CC microcytic anemia, and fatal cardiomyopathy with lactic acidosis
CC following a febrile illness. {ECO:0000269|PubMed:32004446}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Inactive as DHA kinase and FMN cyclase.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000305}.
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DR EMBL; DQ138290; ABA10576.1; -; mRNA.
DR EMBL; DQ344550; ABC70184.1; -; mRNA.
DR EMBL; AK023915; BAB14722.1; -; mRNA.
DR EMBL; AK223580; BAD97300.1; -; mRNA.
DR EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001341; AAH01341.1; -; mRNA.
DR CCDS; CCDS8003.1; -. [Q3LXA3-1]
DR RefSeq; NP_056348.2; NM_015533.3. [Q3LXA3-1]
DR RefSeq; XP_016873010.1; XM_017017521.1.
DR RefSeq; XP_016873012.1; XM_017017523.1.
DR AlphaFoldDB; Q3LXA3; -.
DR SMR; Q3LXA3; -.
DR BioGRID; 117481; 83.
DR DIP; DIP-60967N; -.
DR IntAct; Q3LXA3; 10.
DR STRING; 9606.ENSP00000378360; -.
DR GlyGen; Q3LXA3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q3LXA3; -.
DR PhosphoSitePlus; Q3LXA3; -.
DR BioMuta; TKFC; -.
DR DMDM; 311033370; -.
DR REPRODUCTION-2DPAGE; IPI00551024; -.
DR CPTAC; CPTAC-188; -.
DR CPTAC; CPTAC-189; -.
DR EPD; Q3LXA3; -.
DR jPOST; Q3LXA3; -.
DR MassIVE; Q3LXA3; -.
DR MaxQB; Q3LXA3; -.
DR PaxDb; Q3LXA3; -.
DR PeptideAtlas; Q3LXA3; -.
DR PRIDE; Q3LXA3; -.
DR ProteomicsDB; 61779; -. [Q3LXA3-1]
DR Antibodypedia; 28186; 191 antibodies from 31 providers.
DR DNASU; 26007; -.
DR Ensembl; ENST00000394900.8; ENSP00000378360.3; ENSG00000149476.16. [Q3LXA3-1]
DR GeneID; 26007; -.
DR KEGG; hsa:26007; -.
DR MANE-Select; ENST00000394900.8; ENSP00000378360.3; NM_015533.4; NP_056348.2.
DR UCSC; uc001nre.4; human. [Q3LXA3-1]
DR CTD; 26007; -.
DR DisGeNET; 26007; -.
DR GeneCards; TKFC; -.
DR HGNC; HGNC:24552; TKFC.
DR HPA; ENSG00000149476; Tissue enhanced (intestine, liver).
DR MalaCards; TKFC; -.
DR MIM; 615844; gene.
DR MIM; 618805; phenotype.
DR neXtProt; NX_Q3LXA3; -.
DR OpenTargets; ENSG00000149476; -.
DR Orphanet; 1369; Congenital cataract-hypertrophic cardiomyopathy-mitochondrial myopathy syndrome.
DR PharmGKB; PA142672014; -.
DR VEuPathDB; HostDB:ENSG00000149476; -.
DR eggNOG; KOG2426; Eukaryota.
DR GeneTree; ENSGT00390000015415; -.
DR HOGENOM; CLU_017054_6_2_1; -.
DR InParanoid; Q3LXA3; -.
DR OMA; TALNMNG; -.
DR OrthoDB; 472175at2759; -.
DR PhylomeDB; Q3LXA3; -.
DR TreeFam; TF313821; -.
DR BRENDA; 2.7.1.28; 2681.
DR BRENDA; 2.7.1.29; 2681.
DR BRENDA; 4.6.1.15; 2681.
DR PathwayCommons; Q3LXA3; -.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-70350; Fructose catabolism.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q3LXA3; -.
DR BioGRID-ORCS; 26007; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; TKFC; human.
DR GeneWiki; DAK_(gene); -.
DR GenomeRNAi; 26007; -.
DR Pharos; Q3LXA3; Tbio.
DR PRO; PR:Q3LXA3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q3LXA3; protein.
DR Bgee; ENSG00000149476; Expressed in right adrenal gland cortex and 133 other tissues.
DR ExpressionAtlas; Q3LXA3; baseline and differential.
DR Genevisible; Q3LXA3; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034012; F:FAD-AMP lyase (cyclizing) activity; IDA:UniProtKB.
DR GO; GO:0004371; F:glycerone kinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050354; F:triokinase activity; IDA:UniProtKB.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; IEA:Ensembl.
DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IDA:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; IDA:UniProtKB.
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 Alternative splicing; ATP-binding; Cataract; Cobalt; FAD; Flavoprotein;
KW Kinase; Lyase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..575
FT /note="Triokinase/FMN cyclase"
FT /id="PRO_0000121525"
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 REGION 348..367
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 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:0007744|PubMed:24275569"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KLZ6"
FT VAR_SEQ 526..575
FT /note="SAEAAAEATKNMEAGAGRASYISSARLEQPDPGAVAAAAILRAILEVLQS
FT -> EGGGLVICP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_057181"
FT VARIANT 185
FT /note="A -> T (in dbSNP:rs2260655)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16289032, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_028108"
FT VARIANT 334
FT /note="A -> G (in dbSNP:rs35723406)"
FT /id="VAR_054780"
FT VARIANT 445
FT /note="G -> S (in TKFCD; very severe decrease of triokinase
FT and glycerone kinase activities; dbSNP:rs1590578831)"
FT /evidence="ECO:0000269|PubMed:32004446"
FT /id="VAR_083849"
FT VARIANT 543
FT /note="R -> I (in TKFCD; reduced protein levels in patient
FT cells; very severe decrease of triokinase and glycerone
FT kinase activities; dbSNP:rs547013163)"
FT /evidence="ECO:0000269|PubMed:32004446"
FT /id="VAR_083850"
FT MUTAGEN 112
FT /note="T->A: Highly decreases kinase activity. No effect on
FT FMN cyclase activity."
FT /evidence="ECO:0000269|PubMed:24569995"
FT MUTAGEN 204
FT /note="K->A: Slightly decreases kinase activity. No effect
FT on FMN cyclase activity."
FT /evidence="ECO:0000269|PubMed:24569995"
FT MUTAGEN 221
FT /note="H->A: Abolishes kinase activity but not FMN cyclase
FT activity."
FT /evidence="ECO:0000269|PubMed:24569995"
FT MUTAGEN 401
FT /note="D->A: Abolishes both kinase and FMN cyclase
FT activities."
FT /evidence="ECO:0000269|PubMed:24569995"
FT MUTAGEN 403
FT /note="D->A: Abolishes both kinase and FMN cyclase
FT activities."
FT /evidence="ECO:0000269|PubMed:24569995"
FT MUTAGEN 404
FT /note="C->A: Decreases both kinase and FMN cyclase
FT activities."
FT /evidence="ECO:0000269|PubMed:24569995"
FT MUTAGEN 446
FT /note="S->A: Decreases both kinase and FMN cyclase
FT activities."
FT /evidence="ECO:0000269|PubMed:24569995"
FT MUTAGEN 556
FT /note="D->A: Abolishes both kinase and FMN cyclase
FT activities."
FT /evidence="ECO:0000269|PubMed:24569995"
FT CONFLICT 7
FT /note="V -> A (in Ref. 3; BAB14722)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="A -> S (in Ref. 4; BAD97300)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="V -> A (in Ref. 3; BAB14722)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="L -> P (in Ref. 3; BAB14722)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="D -> G (in Ref. 3; BAB14722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 58947 MW; 4DB8C5326F65122C CRC64;
MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ
VNVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL
MLDHMTNTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV
GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAAAWPNVA AVSITGRKRS RVAPAEPQEA
PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIQEWLK
EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG
AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS
