ID A0A132AHG5_SARSC Unreviewed; 991 AA.
AC A0A132AHG5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=QR98_0089960 {ECO:0000313|EMBL:KPM10441.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM10441.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM10441.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM10441.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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}.
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:KPM10441.1}.
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DR EMBL; JXLN01015162; KPM10441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AHG5; -.
DR VEuPathDB; VectorBase:SSCA002131; -.
DR OMA; SIHCQLQ; -.
DR OrthoDB; 1211169at2759; -.
DR UniPathway; UPA00131; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02940; DHPD_FMN; 1.
DR Gene3D; 3.30.70.20; -; 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; 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; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364041}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ SEQUENCE 991 AA; 109740 MW; 9DE52F67D381A946 CRC64;
MENHKLLSVD SADIEDILKL NPKIKEWASV LPSLVTKSEK FRWKRNKDRC DWKDLRNNFD
DIKHTTLSER GALREAARCL KCADAPCQKS CPTQLDIKAF IGMIANRNYY GAARCILADN
PLGLTCGMVC PTSNLCVGGC NLYATEEGPI NISGLQHFAM EVFRKMNVRQ IRDPNLPPPE
EMPEVFKSKI ALIGCGPASI SCATFLARLG YTDLTIMEKD EWLGGLSATE IPQFRLPFQA
VKFEIDLMLD LGVKIVTNRA LGYDFTLEQL KNLHQFECVF LGIGLPQPKL DSIFIDLSER
NGFFTSKSFL PKVAKASKQT DMKESTNSCT ACNRLPELDG TVIVLGAGDT AFDCATSAIR
CGAKKVYVVF RRGFHNMRAV KEEIDLAYEE KCEFMPFMSP FRVNLDDHHH IESLEFYRTE
VNEQNHLKED CDQKIELKCQ FVIAAFGSTL SDPNVQKALQ PLEFKPNGLP VVDNHTMTTS
EPWVFCGGDL AGVSETTVEA VNDGKTAAWS IHRFLHQKYH EPIVDEIARL PTMFTAIDLV
DLSIEICGLK FSNPFGLASA PPTTSGSMIR RAFEAGWAFA ITKTFGLDKD SVTNVSPRII
RGSTSGHLYG PHISSFLNIE LISEKRAAYW CRIIAELKRD FPDRILIASI MAKYNREDWN
DLALMASETG ADALELNLSM GLACGQNPQM VEDICRWVKS RVKIPVFAKL TPNVTDIIQI
AKAAHQGGAD GVTVINTVSS LMWLRGDGSP WPNIGREART TYGGMSGSAI RPMALRAVSA
ISHAVPELTI LATGGIDSAE SGLQFLYAGA SAFQICSAVQ NQDFTIIQDY ISGLKTLLYL
KSLNDKEYEK NWNFQSPPTP IHQKGKPIRG KPFCDSALSG DRNLSSKHSI INLKSLVGSS
LSKIGTFNQL DVKEQKVALI NQDMCINCGK CYMTCNDSGY QAIVFDNLTH LPKVTDDCTG
CTLCYSVCPI IDCIAMVPKL KPHHVKRGVL T
//
