ID G1QPV1_NOMLE Unreviewed; 575 AA.
AC G1QPV1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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|Ensembl:ENSNLEP00000002967.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000002967.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000002967.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000002967.1}
RP IDENTIFICATION.
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 EMBL; ADFV01078994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003274084.1; XM_003274036.3.
DR RefSeq; XP_012351739.1; XM_012496285.1.
DR AlphaFoldDB; G1QPV1; -.
DR STRING; 61853.ENSNLEP00000002967; -.
DR Ensembl; ENSNLET00000003119.2; ENSNLEP00000002967.1; ENSNLEG00000002383.3.
DR GeneID; 100591351; -.
DR KEGG; nle:100591351; -.
DR CTD; 26007; -.
DR eggNOG; KOG2426; Eukaryota.
DR GeneTree; ENSGT00390000015415; -.
DR HOGENOM; CLU_017054_6_2_1; -.
DR InParanoid; G1QPV1; -.
DR OMA; ALNMNGF; -.
DR OrthoDB; 6043at2759; -.
DR TreeFam; TF313821; -.
DR Proteomes; UP000001073; Chromosome 4.
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; IEA:Ensembl.
DR GO; GO:0050354; F:triokinase activity; IEA:Ensembl.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IEA:Ensembl.
DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; IEA:Ensembl.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IEA:Ensembl.
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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000001073};
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 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: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 575 AA; 59033 MW; BDA9664BBAB25291 CRC64;
MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEITKQ
VNVVAKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL
MLDHMTNTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV
GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTVAAWPNVA AVSITGRKRS RVAPAEPQEA
PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIREWLK
EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG
AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS
//
