ID A0A0K0DYG4_STRER Unreviewed; 1058 AA.
AC A0A0K0DYG4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000228000.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000228000.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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|ARBA:ARBA00001917,
CC 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 AlphaFoldDB; A0A0K0DYG4; -.
DR STRING; 6248.A0A0K0DYG4; -.
DR WBParaSite; SSTP_0000228000.1; SSTP_0000228000.1; SSTP_0000228000.
DR UniPathway; UPA00070; -.
DR UniPathway; UPA00131; -.
DR Proteomes; UP000035681; 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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02940; DHPD_FMN; 1.
DR Gene3D; 3.30.70.20; -; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
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; PF14697; Fer4_21; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00912; DHODEHASE_2; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364041};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 961..993
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 994..1024
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1058 AA; 115876 MW; 8DEE9E3722D01983 CRC64;
MAPQNFEKFS QDSPDIEAIL ALNPRVNTHA KAIPTIETKK NKLNWKRNSP KGCNIKSCNN
GSNPYEKDFR DIKHTTLSER AALRESARCL KCADAPCQKS CPTSLDIKAF ITSISNKNYY
GAAKQIFSDN PLGLTCGMIC PTSDLCVGGC NLAASEEGPI NIGGLQQFAT DVFRQMNIKQ
KVSPEVELST NDNPSYKEKI ALIGCGPASI SCATFLARLG YKDITIYEKN SDPSIIGGLS
TTEIPQFRLP YNVVDFEIQL MKDLGVKIVN GRYLHSSDLT VSNIKEKLGA KALFIGIGMP
EAKRIPIFEG LTIENGFYTS KDYLPIVAKG SKPGMCTCSS SSLPSFVGYR VLVLGAGDTA
FDCATSALRC GAAKVTVVFR KGFTDIRAVP EEMEAAKEEK CEFMPYMSPR KVNMKDNKIY
SMTFVKTEQD LTTGEWYEDE EQVLTLKADI VISAFGSTLI DKDVIEALSP IKLNKWGTPE
VDYKTQSTSE PWVYVGGDFG GIAETTVESV NDGKVAAWNI HKYLQKQYNI NISSKPQLPL
FYTSIDDVDT SVTLCGIKFE NPFGLASAPP TTSGPMIRRA FEQGWGFVLT KTFGLDKDLV
TNVSPRIVRG TTSGHIYGPG QGSFINIELI SEKKMAYWLK CIEELKKDFP TKVIIASIMC
SFNKEDWQEL AIASEKSGAD ALELNLSCPH GMGERGMGLA CGQDPYMVEN ICKWVREVTT
IPFFAKMTPN ITDIRKIAQA AKDGGADGVT ATNTVSGLMS LKSGDGSPWP AVGSEKRTTY
GGMSGNAIRP IALRAVSAIA NAIPGFPILA TGGIDSADAA VQFLYAGASV VQICSSVQNQ
DFSVIGDYII GLKALLYLNS IETFQHNGWD GQSPPIFSHQ MGKRILIENT KIPNFGKFKD
EKKKLEKNVI MNQNLIEKKA EDFATRNNYK ESTKIPTVNE IIGLSLKMIG SYNELTNKEQ
KVALINDDMC INCGKCYMTC ADSGYQAITF DPITHIPCVT DDCTGCTLCY SVCPIPECIQ
MIEKKIPHKI KRGYPLNSYE TLTKSSNGKI ILNPNNAD
//
