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Database: UniProt
Entry: T1A703_9ZZZZ
LinkDB: T1A703_9ZZZZ
Original site: T1A703_9ZZZZ 
ID   T1A703_9ZZZZ            Unreviewed;       438 AA.
AC   T1A703;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=B1A_17818 {ECO:0000313|EMBL:EQD36669.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD36669.1};
RN   [1] {ECO:0000313|EMBL:EQD36669.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD36669.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
CC   -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010804}.
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:EQD36669.1}.
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DR   EMBL; AUZX01013118; EQD36669.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1A703; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd02940; DHPD_FMN; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
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   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   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          337..369
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          372..402
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   438 AA;  47951 MW;  5546FD1B4A0502AF CRC64;
     MADLHTKFLG IQSPNPFWLA SAPPTDKEIN VIRAFEAGWG GVIWKTLGEN PPVVNINGPR
     YSALMSQDRR VIGFNNIELI SDRALETNLE EIRHVKRLWP DRAMVVSLMV PCEEQSWKQI
     ISMVEDTGAD GIELNFGCPH GMNERGMGAA VGQVPEYIEM VTAWCKQYSK LPVIVKLTPN
     ITDVRFPARA AKAGGADAVS LINTINSIMG VDIERMVMFP NTDGKGAHGG YCGPAVKPIA
     LHMVAEIARD PETVGLPISG IGGVTTWRDA AEYISLGCGT VQVCTAAMVY GFKIVQDMCD
     GLSNFMDDQG YASIAEFQGR AIPSVVDWRE LNLNHVEKAV IDQNLCIKCG RCYVVCEDTS
     HQAITAQQNG ARHYEIKEEE CVGCNLCVSI CPVPNCINMR SLKPGEIDRR TGQVVSGNYA
     NWTTHPNNPN ALRNTAEI
//
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