ID A0A2G5TEX5_9PELO Unreviewed; 567 AA.
AC A0A2G5TEX5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, 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 Name=Cni-W02H5.8 {ECO:0000313|EMBL:PIC25621.1};
GN Synonyms=Cnig_chr_V.g18482 {ECO:0000313|EMBL:PIC25621.1};
GN ORFNames=B9Z55_018482 {ECO:0000313|EMBL:PIC25621.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC25621.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC25621.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDUG01000005; PIC25621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TEX5; -.
DR STRING; 1611254.A0A2G5TEX5; -.
DR Proteomes; UP000230233; Chromosome v.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..328
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 361..557
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 520..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 54..57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 567 AA; 60685 MW; 0F3988107D768599 CRC64;
MSKKFVNKLE ETVDDALFGL VGSNKDVQFC KTSKRVIHRS QVNTENVSLI AGGGSGHEPY
AAGYVGKGLL TAAVAGNIFA SPPSRNVQTA LEVTKGKAGA ILFVINYTGD RLNFGLAAER
FNASGGNSRV VTISDDVAID NPNNRVGRRG LAGAVLTIKI AGAMSEEGRS LDEIYDMSQK
VVNSMGTLGV SLYPGSLPGK DRETDMSKDQ IEIGLGIHGE PGKFRASYES AHKIISGLMG
TLKAKMEMKE SDEFVVLVNN LGSVSQLEMG IVNGEVLRWF EMEKMKVARF YSGTYMTSLD
GHGISVTVLR ADKSMIKYLD APANAPGWIP SLSHRNKAQQ PHADKNAPIE VESTGTSIHP
DLARECLNGV VKSMMDSEDQ LNTLDAQSGD GDCGSTFASA ARAIQKADKL DYEHPETLLK
QLSVIFEQTV GGTSGALYAL MFSAAAPELH EKIESNTILE ALKKANHAVQ KYGGARVGDR
TMVDALDAMV EDLGKGLADN GGLDVFERAI QASENAAKET AHQKASVGRA SYTSSESQTK
PDAGAAAISI WFRAFWTAFK EEMGKNI
//
