ID A0A3P8ZNU8_ESOLU Unreviewed; 569 AA.
AC A0A3P8ZNU8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 24.
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};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000030529.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000030529.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000030529.2}
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 AlphaFoldDB; A0A3P8ZNU8; -.
DR Ensembl; ENSELUT00000008101.2; ENSELUP00000030529.2; ENSELUG00000007754.2.
DR GeneTree; ENSGT00390000015415; -.
DR OrthoDB; 6043at2759; -.
DR Proteomes; UP000265140; LG24.
DR Bgee; ENSELUG00000007754; Expressed in ovary and 15 other cell types or tissues.
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:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
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:UP000265140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..338
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 372..567
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT ACT_SITE 223
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 58..61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 569 AA; 59171 MW; 42CBB18A0FD974AA CRC64;
MEPLQRKLLN AVDHCVDEAL EGIVSSSGCL SLLRGHRVVV RADLGALRGQ VGLVSGGGSG
HEPAHTGFIG GGMLSAAVAG GVFASPPPAS VLAAILALRD AGASGVLLIV KNYTGDRLNF
GLAVEQARNR GVAVDMVIVA DDCAFSQPSK AGRRGLCGTV FVHKLAGALA AEGRPLEEIV
CQVKEALKNI GTLGVSLSPC SVPGCLPSFD LPPGEMELGL GIHGEPGIKR LKVATADEVV
NNMIDHMTNP ASQSHLALKS GDSVVLCVNN LGALSRLEMA VVTRAAINCL EGRGVQVARV
MSGSFMTSLE MAGVSLSLMK ANQEVLRLFD AKTSAPAWPN QSGVRVSGRS YTLDPPAVGT
DVSSQSEGPL SGVMANTLEM VCSSLLQRQE ELNSLDRASG DGDCGNTHAQ AAKAILEWLH
SHVVPGCPGQ LMSTLAGLVQ ERMGGSSGAL YSLFLTAAAV PLKDHCHPAA WATAMHAGTE
AIRRYGGADP GDRTMVRTPK MVPYTNLPFL CVTHSPCLSF QRSELGAEST RDLIARAGRA
SYIATERVTL PDPGAVAIAT ILRAVFQSE
//
