ID A0A2J7Q6C5_9NEOP Unreviewed; 891 AA.
AC A0A2J7Q6C5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 Name=DPYD_1 {ECO:0000313|EMBL:PNF24143.1};
GN ORFNames=B7P43_G00594 {ECO:0000313|EMBL:PNF24143.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF24143.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF24143.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF24143.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) 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|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:PNF24143.1}.
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DR EMBL; NEVH01017533; PNF24143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7Q6C5; -.
DR UniPathway; UPA00131; -.
DR Proteomes; UP000235965; 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: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_dom.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01037; pyrD_sub1_fam; 1.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01180; DHO_dh; 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|RuleBase:RU364041};
KW FAD {ECO:0000256|RuleBase:RU364041};
KW Flavoprotein {ECO:0000256|RuleBase:RU364041};
KW FMN {ECO:0000256|RuleBase:RU364041}; Iron {ECO:0000256|RuleBase:RU364041};
KW Iron-sulfur {ECO:0000256|RuleBase:RU364041};
KW Metal-binding {ECO:0000256|RuleBase:RU364041};
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:UP000235965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 812..844
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 846..875
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 891 AA; 96573 MW; 2C94E9EECA2E5CAA CRC64;
MVCPTSDLCV GGCNLQAVEE GPINIGGLQQ FATEVFRSMN VPQVRPVNQH NKNSAAKIAL
VGCGPASLSC ATFLARLGYT DITIFEKENY VGGLSSSEIP QYRLPYDVVN FEIDMVKDLG
VKVKTGRALS KHDLSIKGLE KEGYRAVFLG IGLPEPKIIP AFEGLTKEMG FYTSKSFLPS
VAKGSKAGMC ECRSALPSLQ GSVVVLGAGD TAFDCATSAL RCGAKKVFVV FRKGFRNIRA
VPEEVELAQE EKCEFIPFQS PKQVILKENK IVAVEFYRTE QDENGRWIED AEQITRLKAN
FIISAFGSGL YDLEVKDAMA PLRFSKWGLP EVDPNTMQTS ESHVFCGGDL AGTSETTVES
VNDGKTAAWF MHKYLQDLVG VKIPEEPQLP KFCTPIDDVD ISVEMCGMKF INPFGLASAP
PATSSAMIRR AFEAGWAFAV TKTFSLDKDL VTNVSPRIVR GTTSGHQYGP QQGSFLNIEL
ISEKCCAYWC QSIAELKKDF PDKIVIASVM CSYSASDWTE LCQRAETSGA DALELNLSCP
HGMGESGMGL ACGQDPELVL NICRWVRAAI KIPFFIKITP NITDIVSIAR AAYEGGADGV
SAINTLSGLM GLKADASPWP AVGRDRLTTY GGVSGNAVRP VALRAVSAIA SALPGFSIMG
IGGIDSAEAG LQFLHCGASV LQIGSAIQNQ DFTLIDDYIT GLKALLYLKS LEHHSGWDGQ
SPPKAKHQRG KPVVVLQDIR NKKWPYFGHY QSLREEKISE IKKQADLLAE NLKPPLRSCN
EPTKPVPAVK NVIGQALPMI GPYKGLDNKQ QVVALIDDDL CINCGKCYMA CNDSGYQAIT
FDPETHIPTV TDDCTGCILC LSVCPIIDCI SVVPRKIPHV INRGVPSFGY V
//