ID A0A821RHE9_9BILA Unreviewed; 740 AA. AC A0A821RHE9; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 27-MAR-2024, entry version 13. 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}; GN ORFNames=QYT958_LOCUS26596 {ECO:0000313|EMBL:CAF4843208.1}; OS Rotaria socialis. OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria; OC Bdelloidea; Rotaria. OX NCBI_TaxID=392032 {ECO:0000313|EMBL:CAF4843208.1, ECO:0000313|Proteomes:UP000663848}; RN [1] {ECO:0000313|EMBL:CAF4843208.1} RP NUCLEOTIDE SEQUENCE. RA Nowell W R.; RL Submitted (FEB-2021) 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|ARBA:ARBA00001974, CC 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|ARBA:ARBA00004668, ECO:0000256|RuleBase:RU364041}. CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00010804, ECO:0000256|RuleBase:RU364041}. 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:CAF4843208.1}. 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; CAJOBR010006404; CAF4843208.1; -; Genomic_DNA. DR AlphaFoldDB; A0A821RHE9; -. DR UniPathway; UPA00131; -. DR Proteomes; UP000663848; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IEA:UniProt. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH_cat. DR InterPro; IPR028261; DPD_II. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR009051; Helical_ferredxn. DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1. DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1. DR Pfam; PF01180; DHO_dh; 1. DR Pfam; PF14691; Fer4_20; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00419; ADXRDTASE. DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR SUPFAM; SSF51971; Nucleotide-binding domain; 2. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU364041}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU364041}; KW Flavoprotein {ECO:0000256|RuleBase:RU364041}; KW FMN {ECO:0000256|RuleBase:RU364041}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364041}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW NADP {ECO:0000256|RuleBase:RU364041}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU364041}; Repeat {ECO:0000256|ARBA:ARBA00022737}. FT DOMAIN 67..175 FT /note="Dihydroprymidine dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF14691" FT DOMAIN 197..505 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 543..736 FT /note="Dihydroorotate dehydrogenase catalytic" FT /evidence="ECO:0000259|Pfam:PF01180" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CAF4843208.1" SQ SEQUENCE 740 AA; 80911 MW; 9EE71FF20DD627F3 CRC64; MPSENTTEQQ LLSKDPPDIE SLLLLNPRTK PFANSRPSVQ TLQEKKHWKR NDEHSCATGC TKDLSRNFLD VKHTTLSERG ALREAARCLK CADAPCQKSC PTSIDIKSFI TSISNKNYYG AAKAILSDNP LGLTCGMVCP TSDLCVGGCN LHASEEGAIN IGGLQQFAVD IFKSMHIPAI RDPSSEGVPL NEKYSSKIAL IGCGPASISC ATFLGRLGYS DLTIFEKQDF LGGLSSSEIP QYRLPFDTVN FEIELMKDLG VKIIPNKPLT TENDGLTIKN LLNEHGFKAV FLGIGLPNPN IDPIFKDLTK AEGFYTSKNF LPLIAKSSKA GMCACKSALP VMSGNVIVLG AGDTAMDCAT SAIRCGATKV FVCFRKGFNQ MRAVPEEVDV AMEERCEFLP FCSPKQVFVK NGKITSMEFV KTEQTESGDW IEDEDQIIRL KCNYVISAFG STLNEHPVVQ ALAPIQLDKY NYPVVDLTTM TTSEKGVFCG GDIAKVASTT VECVNDGKTA AWHIHRYIQG VETIPLEPQL PKFYTPIDKV DVSVEICGIK FPNPFGLASA PPVTSGPMIR RSFESGWGFV VTKTYCLDKD IITNVSPRIV RGTTSGFNYG PGQGSFLNIE LISEKNTEYW LRCITELKRD FPDRIVIASI MCGYNEADWT ELAKVTESSG ADALELNLSC PHGMGEKGMG LACGQRADLV LNICKWVRAA VKIPFFAKMT PNITNIIDIA RAAKEGKKMN //