ID A0A401SFH2_CHIPU Unreviewed; 653 AA.
AC A0A401SFH2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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 ORFNames=chiPu_0007594 {ECO:0000313|EMBL:GCC29157.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC29157.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC29157.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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};
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:GCC29157.1}.
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; BEZZ01000236; GCC29157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401SFH2; -.
DR STRING; 137246.A0A401SFH2; -.
DR OMA; ALNMNGF; -.
DR Proteomes; UP000287033; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000287033};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..337
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 373..572
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 575..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 372..399
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 588..653
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 57..60
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 653 AA; 68346 MW; 9D4C491AA793BEE9 CRC64;
MHHSKKLINS VENCVDDALD GLVACNVGMQ LLQGHRVIIR ADLKNMKGKV ALLSGGGSGH
EPAHAGYVGV GMLSGAIAGD VFTSPPPGSI SAAIRIMDRA GAAGVLLIVK NYTGDRLNFG
LALEEAKADG IDVEMVIVAD DCAFTTQKKA GRRGLCGTVL IHKMAGTMSE MGMSLCEIVE
KLNVALGKLG TMGICLSPCS VPGSEPTFNL EADELELGLG IHGEAGIERI KMMSANEVVQ
KMIDHMTDPS NESHLNLEAG DHIVLIVNNL GGLSCLELSI VAKSAVKYLE HKEVIIERAY
IGSLMTALEM GGASLTLMIV NSEQLKLLDS RTSAPGWPNA GRHRLVRRCK ILSAPSLEPE
SSLTAAEPGP FVQKAQLVLD KIANTLLQME EELNELDREA GDGDCGVTHA RAANAIRNLL
TSNAVPGNGH QLLLCLGRIV RDHMGGSSGA LYSIALTAAA QCLKDNNNPT AWAAAMSTGI
EALKRYGGAE PGDRTMLDSL CPAADELSKL TDEDGSELQV LANAVQKAEE GAEATKDMAA
KAGRASYISS AQLTRPDAGA VACSAILKAT LAGLEQPAPG EPAPEEPAPE EPAPEEPAPE
EPAPEEPAPE ESAPEESAPE EPAAEEPAPE EPAPEEPAPE EPAPEDPAPE EQE
//
