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Database: UniProt
Entry: A0A210QXG5_MIZYE
LinkDB: A0A210QXG5_MIZYE
Original site: A0A210QXG5_MIZYE 
ID   A0A210QXG5_MIZYE        Unreviewed;       535 AA.
AC   A0A210QXG5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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   ORFNames=KP79_PYT10501 {ECO:0000313|EMBL:OWF53403.1};
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF53403.1, ECO:0000313|Proteomes:UP000242188};
RN   [1] {ECO:0000313|Proteomes:UP000242188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX   PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA   Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA   Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA   Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA   Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA   Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA   Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA   Chourrout D., Li R., Bao Z.;
RT   "Scallop genome provides insights into evolution of bilaterian karyotype
RT   and development.";
RL   Nat. Ecol. Evol. 1:120-120(2017).
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:OWF53403.1}.
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DR   EMBL; NEDP02001349; OWF53403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A210QXG5; -.
DR   STRING; 6573.A0A210QXG5; -.
DR   EnsemblMetazoa; XM_021491628.1; XP_021347303.1; LOC110446463.
DR   Proteomes; UP000242188; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242188};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..286
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          329..531
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
SQ   SEQUENCE   535 AA;  57108 MW;  CDAF794A53380C38 CRC64;
     MNNSQLLVCI FIVSYYMLSY QELNFFCVDL DKLIFLTKPI KYEFSFRWSA GVLLIIKNYT
     GDRLNFGMSA ERAKSQLGVK VEMVVVGEDC ALTSSDKTAG RRGLCGTLFI HKICGALSDE
     GKSLEEIVKL AKDAASKMGT IGLSLTPCSI PGSGPSFQIA DDEMELGLGV HGEAGVKRTK
     LVSAKEAVKM MIDHMTNPSN CTHLPVKKGD RVACMINNLG GTSMLELNII AKETIELLES
     RGVVVERAYC GTFITSLEMA GISITLLHLD DTLRRCLDAP TTAPAWPRPL LPCGTMTRKT
     PVRMPREDIQ AKVTKTGPKM ATVESAEASL IHDCLKLAGE RLVAAESQLN ELDRESGDGD
     CGSTMARGAH GILASLGSKE NPKLPISCPG GLALTLASAA EDTMGGSSGG LYSLFFTAAS
     TCLQTTVSPN TYCDALIAGI QTMMKYGGAE PGDRTMLDPL HSASQAWSAA LSSHSPLDAF
     HLAVEAAEKS AEETVTMKAQ AGRASYVSAD HLKHPDPGAR AVAIWMRAVL EALTS
//
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