ID A0A182V481_ANOME Unreviewed; 1039 AA.
AC A0A182V481;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-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};
OS Anopheles merus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM008565-PA, ECO:0000313|Proteomes:UP000075903};
RN [1] {ECO:0000313|Proteomes:UP000075903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles merus MAF (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEM008565-PA}
RP IDENTIFICATION.
RC STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM008565-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; A0A182V481; -.
DR STRING; 30066.A0A182V481; -.
DR EnsemblMetazoa; AMEM008565-RA; AMEM008565-PA; AMEM008565.
DR VEuPathDB; VectorBase:AMEM008565; -.
DR VEuPathDB; VectorBase:AMEM21_012002; -.
DR OrthoDB; 1211169at2759; -.
DR UniPathway; UPA00131; -.
DR Proteomes; UP000075903; 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: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; 1.
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}.
FT DOMAIN 952..984
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 986..1015
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1039 AA; 112483 MW; AB1E2FE6B5500498 CRC64;
MSCASVLTSK DLPDIESLLA LNPRVKQSCS LVPTTVTKKV KKHWKRNEDR SCTSCTPLTN
DFSDIKHTTL SERAALKEAA RCLKCADAPC QKSCPTQLDI KSFITSIANR NYYGAAKAIF
SDNPLGLTCG MVCPTSDLCV GGCNLAAVEE GPINIGGLQQ FATEVFKRMG LRQIVPPGVA
PLKHPNKRIA LLGGGPASLS CATFLGRLGY RDVTVYERRP YLGGLSSAEI PQYRLPVEVV
NFEVDLVKDL GVRFELNRAL SAQDLTVRGL LDGGVDAVFL GIGLPQPKVD RVFEGLTEEH
GFYTSKSFLP QVADGSKPGL CGCKQSAKLP TLHGNVIVLG AGDTAFDCAT SALRCGARKV
FVVFRKGNNN IRAVPEEVEL AREERCEFIP FMAPREVIVR AGRIAAMEFY RTEQDETGNW
VEDQDQITRL KANYIISAFG SGLYDADIIS ALDGLKMNRW GLPEVDPKTQ QTSLPAVFCG
GDLAGAAETT VESVNDGKTA AWYMHCYLQG IPLDAKPELP LFYTEIDKVD LSVEVCGVRF
ENPFGLASAP PTTSTAMIRR AFEQGWGFAV TKTFALDKDM VTNVSPRIVR GVTAGQHYGP
QQGAFLNIEL ISEKCCDYWL TGIRELKREF PSRVLIASIM CTYSEPDWVE LASRAEAAGA
DMLELNLSCP HGMGESGMGL ACGQDPELVY NISRWVRGAV RIPFFVKLTP NITDIVSIAQ
AAKRGQADGV SAINTVQGLM SLRADGSPWP AVGADRRTTY GGVSGNATRP QAMRAISLIA
NKLPGFPICG IGGIDSAEVA LQFIQCGAPI LQICSSVQNQ DFTVIEDYIL GLKALLYLRA
NPPPEALPWD GQSPPAAKLQ KGKPVAPLRA EDGKPLLHFG EYKKQREEKL AQLRLQHGPL
WDPCAPEPGT NGHTPDRNEP ATPAAVPRVK DVLGGALPRI GDYKKLDNTK QVVALIDDDL
CINCGKCYMT CADSGYQAIE FDPVTHLPHV NDDCTGCNLC LSVCPIIDCI SMVPKKIPHV
IKRGRPNGSV AVHALSPSQ
//
