GenomeNet

Database: UniProt
Entry: F4W7H7_ACREC
LinkDB: F4W7H7_ACREC
Original site: F4W7H7_ACREC 
ID   F4W7H7_ACREC            Unreviewed;       585 AA.
AC   F4W7H7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=G5I_01393 {ECO:0000313|EMBL:EGI69850.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI69850.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) 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   ---------------------------------------------------------------------------
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; GL887844; EGI69850.1; -; Genomic_DNA.
DR   RefSeq; XP_011067578.1; XM_011069276.1.
DR   AlphaFoldDB; F4W7H7; -.
DR   STRING; 103372.F4W7H7; -.
DR   EnsemblMetazoa; XM_011069276.1; XP_011067578.1; LOC105154032.
DR   GeneID; 105154032; -.
DR   KEGG; aec:105154032; -.
DR   eggNOG; KOG2426; Eukaryota.
DR   InParanoid; F4W7H7; -.
DR   OrthoDB; 6043at2759; -.
DR   Proteomes; UP000007755; 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:EGI69850.1};
KW   Lyase {ECO:0000313|EMBL:EGI69850.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..338
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          377..578
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
SQ   SEQUENCE   585 AA;  63399 MW;  AA7DA144D26923CB CRC64;
     MATSKSLINL LDDAVFETLS GLSYTYPQLE HHASHRVVLS PDHRDRKDKV ALICGGGSGH
     EPFAAGFVGS GMLTASVAGS IFTAPPSIHI TYALQCIAEN NKDGIVVVVP NYTGDRLNFG
     IAIEKTRQAG VAVEEVIVDD DCSIPVNEQS VAGKRGLVGM LFVIKIAGAF AEKGFPLCEV
     AEIARRVSQN TATYGIGLSA CAIPGQGLMF ELAQDEIECG MGVHGEAGYE RIKLRTASEL
     VMLMLKRICE VLSLSTNDSV AVIVNNFGAL SQLEQGIIVY EVVNQLQKTG IQPVRVYSGV
     LMTSLNSVGI HISLLKLTEN HGDVFVDCLD EKTTAPCWPG CTYSISSTST PLSTPLKDAK
     KEKVEKIGIL LNVTDQRLIK LCLKNACIAI IEKEAYLNGL DRGCGDGDCG STLKRFANGI
     LNNLENLSLS HPAALLLEIA NIAEECMGGT SGALYCLFFT TGAKMLASFR QEKDMRNVWF
     CAFRSGLNCL EKYGRAKVGD RTMIDTMYAT YTTYEKLLKE CPSDFYEKIT AAAWEGCYST
     RNMKPKAGRA SYIKQAQYLT EMDAGAYAAA IWIAAIVQTI THFKK
//
DBGET integrated database retrieval system