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Database: UniProt
Entry: N1PBC8_CAPTE
LinkDB: N1PBC8_CAPTE
Original site: N1PBC8_CAPTE 
ID   N1PBC8_CAPTE            Unreviewed;      1026 AA.
AC   N1PBC8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=CAPTEDRAFT_161594 {ECO:0000313|EMBL:ELU18829.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELU18829.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELU18829.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELU18829.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP161594}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-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   EMBL; AMQN01000026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB291798; ELU18829.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1PBC8; -.
DR   STRING; 283909.N1PBC8; -.
DR   EnsemblMetazoa; CapteT161594; CapteP161594; CapteG161594.
DR   HOGENOM; CLU_003991_0_0_1; -.
DR   OMA; AWSIHCQ; -.
DR   UniPathway; UPA00131; -.
DR   Proteomes; UP000014760; 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; IPR028261; DPD_II.
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; 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|RuleBase:RU364041};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000014760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          942..974
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          976..1005
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1026 AA;  111588 MW;  E43A79DBB98F91D0 CRC64;
     MSDVSKDVDD IESILSLNPR IKPFANHKAS AQTKKDKKHW KRNVDQACTT CEPLVQNFDD
     IKHTTLSERG ALKESARCLK CADAPCQKSC PTQLDVKSFI TSISNKNYYG SAKAILSDNP
     LGLTCGMVCP TSDLCVGGCN LYASEEGPIN IGGLQQFAVE GFKEMRIPQI RDPSLPKKSE
     LPETYRAKIA MIGCGPASIS CATFLARLGY SDITVFERRP FVGGLSSSEI PQFRLPYDVV
     NWEVELMKDL GVKIECGKSL DSNGGLTLQG LRNSGYQAVF LGIGLPDPKK LPLFQDLTEQ
     MGFYTSKDFL PKVSAASKPG MCSCKSKLPN LSGTVVVLGA GDTAFDCATS ALRCGAKRVF
     VVFRKGFTNI RAVPEEMELA REEKCEFMPF MAPYKIHTKN NHISAMEFFR TEQDDNGQWV
     EDKEQMIRLK ADFVISAFGS GLTEKNVVEA LEPLKLNRWG LPDVDPTQMT TSEPWVFSGG
     DIAGVAQTTV ESVNDGKTAS WYMHKYLQSL GKLEVPKIAT LPKFFTPIDN VDVSITMCGI
     RFENPFGLAS APPTTTPAMI RRAFEAGWGF ALTKTFSLDK DLVTNVSPRI VRGTTSGQVF
     GPGQGSFLNI ELISEKTAAF WCKGVKELKR DFPTKVVIAS IMSSFNKDDW TELAIMAEAS
     GADALELNLS CPHGMGERGM GMACGQDPNL VLNICRWVRA AVKIPFFAKL TPNVTNVTVI
     AKAAKDGGAD GVTATNTVSG MMGLKQDGAA WPNIGKEKRT TYGGMSGNAI RPIALRAVSA
     IGNALPGYPI LATGGIDCAE VGMQFLYAGA SVLQVCSAVQ NQDYTLIDDY ITGLKCLLYL
     QSLELAGWDG QSPPTPAHQL GKPVPAVKDI VGQSLPNFGP YLQKKNELIA QQKKGADILE
     DHKPPMRNVL VPQKPIPSVQ DMVGKALARI GAYNDLDNQQ QVVALIDEDM CINCGKCYMT
     CNDSGYQAVE FDPETHLPKV NDNCTGCTLC LSVCPIIDCI RMVTRTTPYK PKRGIPPSTK
     HVMVCQ
//
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