ID A0A2K6P8B6_RHIRO Unreviewed; 575 AA.
AC A0A2K6P8B6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSRROP00000012787.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000012787.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000012787.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_010383248.1; XM_010384946.1.
DR STRING; 61622.ENSRROP00000012787; -.
DR Ensembl; ENSRROT00000036909.1; ENSRROP00000012787.1; ENSRROG00000030683.1.
DR Ensembl; ENSRROT00000036912.1; ENSRROP00000012790.1; ENSRROG00000030683.1.
DR GeneID; 104679394; -.
DR KEGG; rro:104679394; -.
DR CTD; 26007; -.
DR GeneTree; ENSGT00390000015415; -.
DR OMA; ALNMNGF; -.
DR OrthoDB; 6043at2759; -.
DR Proteomes; UP000233200; Unplaced.
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:UP000233200};
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 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; 59096 MW; FA2C1F9FA9DBFB77 CRC64;
MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE
PAHAGFIGKG MLTGVVAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL
AREQAQTEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEITKQ
VNMVAKAIGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL
MLDHMTDTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADAAVRSLEG RGVKIARALV
GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAVAWPNVA AVSITGRKRN RVAPAEPQEA
LDSTAVGGSA SKRMALVLER VCSTLLGLEE QLNALDRAAG DGDCGTTHSR AARAIREWLK
EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKVKTSLPA WSAAMDAGLE
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG
AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS
//
