ID A0A3P6HTM8_9CEST Unreviewed; 662 AA. AC A0A3P6HTM8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 02-DEC-2020, entry version 8. DE RecName: Full=Dihydropyrimidine dehydrogenase [NADP(+)] {ECO:0000256|RuleBase:RU364041}; DE Short=DHPDHase {ECO:0000256|RuleBase:RU364041}; DE Short=DPD {ECO:0000256|RuleBase:RU364041}; DE EC=1.3.1.2 {ECO:0000256|RuleBase:RU364041}; DE AltName: Full=Dihydrothymine dehydrogenase {ECO:0000256|RuleBase:RU364041}; DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|RuleBase:RU364041}; DE Flags: Fragment; GN ORFNames=MCOS_LOCUS4629 {ECO:0000313|EMBL:VDD78626.1}; OS Mesocestoides corti. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda; OC Eucestoda; Cyclophyllidea; Mesocestoididae; Mesocestoides. OX NCBI_TaxID=53468 {ECO:0000313|EMBL:VDD78626.1, ECO:0000313|Proteomes:UP000267029}; RN [1] {ECO:0000313|EMBL:VDD78626.1, ECO:0000313|Proteomes:UP000267029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Pathogen Informatics; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes the CC reduction of uracil and thymine. {ECO:0000256|RuleBase:RU364041}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5,6-dihydrouracil + NADP(+) = H(+) + NADPH + uracil; CC Xref=Rhea:RHEA:18093, ChEBI:CHEBI:15378, ChEBI:CHEBI:15901, CC ChEBI:CHEBI:17568, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.2; CC Evidence={ECO:0000256|RuleBase:RU364041}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|RuleBase:RU364041}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|RuleBase:RU364041}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|RuleBase:RU364041}; CC Note=Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms CC per subunit. {ECO:0000256|RuleBase:RU364041}; CC -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis. CC {ECO:0000256|RuleBase:RU364041}. CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family. CC {ECO:0000256|RuleBase:RU364041}. 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; UXSR01001967; VDD78626.1; -; Genomic_DNA. DR UniPathway; UPA00131; -. DR Proteomes; UP000267029; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01180; DHO_dh; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|RuleBase:RU364041}; KW FAD {ECO:0000256|RuleBase:RU364041}; KW Flavoprotein {ECO:0000256|RuleBase:RU364041}; KW FMN {ECO:0000256|RuleBase:RU364041}; Iron {ECO:0000256|RuleBase:RU364041}; KW Iron-sulfur {ECO:0000256|RuleBase:RU364041}; KW Metal-binding {ECO:0000256|RuleBase:RU364041}; KW NADP {ECO:0000256|RuleBase:RU364041}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU364041}; KW Reference proteome {ECO:0000313|Proteomes:UP000267029}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}. FT DOMAIN 2..301 FT /note="Pyr_redox_2" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 349..653 FT /note="DHO_dh" FT /evidence="ECO:0000259|Pfam:PF01180" FT NON_TER 662 FT /evidence="ECO:0000313|EMBL:VDD78626.1" SQ SEQUENCE 662 AA; 71327 MW; C2D2B157A491F885 CRC64; MIGCGPASIS CATYLARLGY RNVHIFERDS RVGGLSTSEI PQFRLPGSAV NFEVQLLLDL GVKIFTNRAF SASEANGITL SSLRKEGYKA IFLGFGLPNA HSTSVFSGLT PDQGYLTSKD FLPEVSSASK GCQGCPKARL PDFSGKRVVV LGAGDTAFDC ATSALRCGAK RVTVSFRKSF TAINPVPEEM DLAWQEKCEF FPNLAPQRVK LGSDGKICEM EFIRREQNDD GSWYSDADQV IRIKTDYVIT AYGSELNEPG VLKAMEGVEL APSGFSKGLP VVDLKSMRTN QEDVWCGGDL SGFAHTSVEA TNDGKTAAWS IHSTLLGDEE SHVTCLPRFT TPIDLVDVSV EMCGMRFENP FGLASAPPTT SSAMIRRAFE AGWGFAVTKT FGLDKELVTN VSPRIVRGPT GGHMYGPDQS GFCNIELISE KTAAYWIQSI KELKRDFPTK MVIASIMAKF DEQDWTQLTE LTVKAKPDAL ELNLSCPHGM GERGMGLACG QDPALVRQIC KWVKRAAGPN MPVFAKLTPN VSEIVEIAKA AREGGADGVT VINTVSGFMH LDSDSTPWPS VGKEKRTTYG GLSGNLIRPM ALRAVSHIAN KLPGFPILAT GGIDSAEAGL QFLQAGASVL QVCSAIQNQD FTIIEDMVTG LKAGLYLDGR EG //