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Database: UniProt
Entry: A0A0V0W1J2_9BILA
LinkDB: A0A0V0W1J2_9BILA
Original site: A0A0V0W1J2_9BILA 
ID   A0A0V0W1J2_9BILA        Unreviewed;       759 AA.
AC   A0A0V0W1J2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=DAK {ECO:0000313|EMBL:KRX69641.1};
GN   ORFNames=T06_11152 {ECO:0000313|EMBL:KRX69641.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX69641.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX69641.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX69641.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX69641.1}.
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DR   EMBL; JYDK01000337; KRX69641.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0W1J2; -.
DR   STRING; 92179.A0A0V0W1J2; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
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; IPR004006; DhaK_dom.
DR   InterPro; IPR004007; DhaL_dom.
DR   InterPro; IPR036117; DhaL_dom_sf.
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, ECO:0000313|EMBL:KRX69641.1};
KW   Lyase {ECO:0000313|EMBL:KRX69641.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          104..437
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          482..686
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
SQ   SEQUENCE   759 AA;  83265 MW;  34C4C6CD6ACCF99F CRC64;
     MLELINSWHN SNATVRVNNF QNGPRKRQQS EMKSKYAATQ IMEACPIISS SIDYIISNIN
     QNISVEMIWF LISVIQKFLN KFLPPRIELL QDDKHNKSRK LLNSASSCVE DNMQSLCMRN
     DKVCKLEKYP VIIRSDLNTV TNVGHVAIIS GGGSGHEPAF GGYVGFGMLT AAVIGEIFTS
     PPSQSILAAL HAVRNAAGVM VVILNYTGDR LHFGVAIERA QRLFPNLPVQ FVVVDDDCAL
     SEVDLMKCRR GLAGSLFLLK IIGAMAEAGE SLQNISVECD LVKKNLSTIG LGLSTCSLPD
     RAPMIDIDQN EMHFGIGIHG ESGMRRIPLM DAKNAVHVMM QTIFTNGFDI KCDDLSDSEK
     LFAVMINSLG SVSQLEMNVV TGEVLQWLMA KGIQVVRVYT GTLMTSIDMH GISISLLRID
     KEEWIDYLDA PTGCHAWPMG TIPSENLDAY ILKYPSMDSL QIIDEGNDLT RNAITVDEKE
     SLEYRNLILT ICNTLKQNEQ KLNYLDSECG DGDCGSTLSK AANIIMVSVE ENLFSTAAPG
     KLFSDIALMM EEKVGGTIGA LLSIFFSAGS ACLMNSTDSL AWFNCFIQGV DAIQFYSGTT
     SGSRTLLDPM KSLADLLSQQ LLFSDGSPVV TGDFMKHLIE NCEIAVEATT KARPKTGRAC
     QVPIELLQKP DAGAYAILLV MNDIVTWSGP MVKSIKAIST TLTDIYLMNN KALTNSKQVK
     NTVALGLEVS RSVFHKLKNV MSNSNKTNKR KGFTQKFPC
//
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