ID   E2ARH7_CAMFO            Unreviewed;       470 AA.
AC   E2ARH7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=EAG_09599 {ECO:0000313|EMBL:EFN63986.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN63986.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010804}.
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DR   EMBL; GL442063; EFN63986.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2ARH7; -.
DR   STRING; 104421.E2ARH7; -.
DR   InParanoid; E2ARH7; -.
DR   OMA; CVGTANR; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT   DOMAIN          40..354
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   470 AA;  52015 MW;  D1D1D0CF268F893E CRC64;
     MTYENSSEIL HFLISHSVFK QMNIPQIRIP NQTVPHANTK IALLGCGPAS LSCATFLARL
     GYNDITIFEK EKYIGGLSSS EIPQYRLPYD AVNFEVDLVR DLGVKIELER SLSEDDLTIQ
     TLQDAGYKAI FLGIGLPESK NIPIFENLML TEKDPTKIGF FTSKSFLPAV AKGSKPGMCA
     CKRQELPSLY GNVIVLGAGD TAFDCATSAL RCGAKKVFVV FRKGFTNVRA VPEEMDLAKE
     EKCEFIPFQS PKQVILRNGK IFAIEFCKTE QNEKGEWIED EEQKFVLKTN FVISAFGSGL
     YSSTVKNAMA PIKINSWNLP EVDENTMMTS VPGVFCGGDL AGVAQTTVES VNDGKTAAWY
     MHKYIQESYG LTVPETPQLP KFHTAIDDVD LSIEMCGLKF ENPFGLASAP PCTTSAMIRR
     AFEAGWAFAV TKTFSLDKDL ITNVSPRIIK GTTSRHHYGP EQSSFLNIEF
//