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Database: UniProt
Entry: F6TNX4_HORSE
LinkDB: F6TNX4_HORSE
Original site: F6TNX4_HORSE 
ID   F6TNX4_HORSE            Unreviewed;       610 AA.
AC   F6TNX4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 67.
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   Name=TKFC {ECO:0000313|VGNC:VGNC:24122};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000013867.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000013867.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000013867.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000013867.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000013867.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000031};
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:0000256|ARBA:ARBA00001015};
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:0000256|ARBA:ARBA00000865};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
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DR   AlphaFoldDB; F6TNX4; -.
DR   STRING; 9796.ENSECAP00000013867; -.
DR   PaxDb; 9796-ENSECAP00000013867; -.
DR   Ensembl; ENSECAT00000017110.3; ENSECAP00000013867.3; ENSECAG00000015944.3.
DR   VGNC; VGNC:24122; TKFC.
DR   GeneTree; ENSGT00390000015415; -.
DR   HOGENOM; CLU_017054_6_2_1; -.
DR   InParanoid; F6TNX4; -.
DR   OMA; ALNMNGF; -.
DR   OrthoDB; 6043at2759; -.
DR   TreeFam; TF313821; -.
DR   Proteomes; UP000002281; Chromosome 12.
DR   Bgee; ENSECAG00000015944; Expressed in adult mammalian kidney and 23 other cell types or tissues.
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:0019563; P:glycerol catabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F6TNX4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..336
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          372..571
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
FT   REGION          577..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        221
FT                   /note="Tele-hemiaminal-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT   BINDING         56..59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ   SEQUENCE   610 AA;  62779 MW;  9AA28842EEF52CD5 CRC64;
     MTSKKLLNSV AGCADDALAG LVACDPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
     PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
     AREQAQAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEITKR
     VSAVAKAMGT LGVSLSSCSV PGSRPTFELS ADELELGLGI HGEAGVRRIK MAAADEIVAL
     MLDHMTNPSN ASHVPVQSGS SVVLMVNNLG GLSFLEVGII ADAAVRSLEG RGVKIARALV
     GTFMSALEMP GISLTLLLVD EPLLKLIDAE TSASAWPNVA KVPVTGRKRS RAAPTEPLEV
     PESTAAGGLA SKQMALVLER VCAALLGLEE HLNALDRAAG DGDCGTTHSR AARAIQGWLK
     EGPPPASPAQ LLSKLSLLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTDLPA WSAAMDAGLE
     AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLFQIL TKAVKSAEAA AEATKDMEAG
     AGRASYISSA RLDQPDPGAV AAAAILRAIL EVLQSQESGA PFHSQTEEKL LVKARNNRRN
     GQREDGGSKE
//
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