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Database: UniProt
Entry: A0A2J7Q6C5_9NEOP
LinkDB: A0A2J7Q6C5_9NEOP
Original site: A0A2J7Q6C5_9NEOP 
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
//
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