ID A0A0R3VY27_TAEAS Unreviewed; 915 AA.
AC A0A0R3VY27;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=TASK_LOCUS2322 {ECO:0000313|EMBL:VDK24858.1};
OS Taenia asiatica (Asian tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000232101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TASK_0000232101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK24858.1, ECO:0000313|Proteomes:UP000282613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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|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}.
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DR EMBL; UYRS01001444; VDK24858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3VY27; -.
DR STRING; 60517.A0A0R3VY27; -.
DR WBParaSite; TASK_0000232101-mRNA-1; TASK_0000232101-mRNA-1; TASK_0000232101.
DR UniPathway; UPA00131; -.
DR Proteomes; UP000046400; Unplaced.
DR Proteomes; UP000282613; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02940; DHPD_FMN; 1.
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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000282613};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 113..213
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 235..549
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 594..898
FT /note="Dihydroorotate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01180"
SQ SEQUENCE 915 AA; 97902 MW; A00ED5638C415202 CRC64;
MYRQAQRVLR RQVELVRVGR RCLACPPVGC GGECSGRGSA KCFSSLNHEE VSRHSAEIEA
VLRLQPKVLT AATVKSTVEI REDKKNWKRN ADKNDSAMLP LHYDFSDAKL TTLGERGALR
EAARCLKCAD APCQHSCPTQ LDVKAFVESI GKKNYYGAAK AILSDNPNGL TCGMVCPTSD
LCVGACNLTA TEEGPINIGG LQQFAVEMFA NMNVPQVVDP AIVARTAGDP HYDTKIALVG
CGPASISCAT FLARLGYRNV HIFERGERLG GLSTTEIPQF RLPGAAVAFE LQLLRDLGVR
IFTGRPFSAS AAEASDSVAA PHGVTLGSLR AAGYKAIFLG FGLPNPHSTG VFAGLTSQQG
FLTSKDFLPC VSAASKGCLG CDNARLPDLK GKRVVVLGAG DTAFDCATSA LRCGASRVTV
SFRKSFTTIN PVPEEMELAW QEKCEFLPNL VPNEVHLGGD GRISELSFVR RERNDDGSWY
TDAEQVVKLK TDVIITAYGA ELDDGDVLSA MEGVTLAPSG FSAGLPVVDP KTMRTNLPDV
WCGGDLTGFA HTSVEATNDG KTAAWSIHST LLDEPDLPMS LPRFTTPIDA VDVSVDVCGV
RFENPFGLAS APPTTSSAMI RRAFEAGWGF AVTKTFGLDK DLVTNVSPRI VRGPTGGHLY
GPDQSGFCNI ELISEKTAAY WIQSIKELKR DFPEKRVIAS IMAKFDEADW REITERTLMA
GPDAVELNLS CPHGMGERGM GMACGQDPRL VREICKWVKS VTGAGVPVFA KLTPNVSDIL
EIAQAAQDGG ADGVTAINTV SGIMHFDSDS SPWPRIGKER RTTYGGLSGN LVRPMALRAV
SWIAKKLPGF PILATGGIDS AEAGMQFLQA GASILQVSSA IQNQDFTIIE DMVTGLKAGL
YLDGREGGFV HFSSI
//
