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Database: UniProt
Entry: A0A1T5DXD4_9SPHI
LinkDB: A0A1T5DXD4_9SPHI
Original site: A0A1T5DXD4_9SPHI 
ID   A0A1T5DXD4_9SPHI        Unreviewed;       422 AA.
AC   A0A1T5DXD4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=SAMN05661099_2701 {ECO:0000313|EMBL:SKB76331.1};
OS   Daejeonella lutea.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Daejeonella.
OX   NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB76331.1, ECO:0000313|Proteomes:UP000189981};
RN   [1] {ECO:0000313|Proteomes:UP000189981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA   Varghese N., Submissions S.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010804}.
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DR   EMBL; FUYR01000002; SKB76331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5DXD4; -.
DR   STRING; 572036.SAMN05661099_2701; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000189981; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189981}.
FT   DOMAIN          334..363
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          370..400
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   422 AA;  46085 MW;  2B555ABCB82CF295 CRC64;
     MADLSSNFLG IKSPNPFWLA SAPPTDKKIN VLRALEAGWG GIVWKTLGSQ VKNVSSRYSA
     VNFHGGKVMG FNNIELISDR PLQINLDEIK EVLRLFPDRA MIVSLMADNS RDSWHELIKK
     VEDTGAHGLE LNFGCPHGMT ERGMGAAVGQ DPEIARMVVE WVMECATVPV ITKLTPNVHS
     VVPTGKAVVE AGTNALSLIN TIQSVTGINL DTLVPNPNVA GKSVFGGYCG PAVKPIALKF
     LTTLGQNELT KNVPVSGIGG VSTWKDAVEF MLLGATNVQV CTAVMTHGFR IIEDLCEGLS
     NWMDEKGFAN ATDFIGKSLP VMTNWEELDI NYHIVANINQ DKCIHCGLCY IACEDTAHQA
     INLSYGTPYN TYSIKEPECV GCNLCSLVCP VDNCITMIEQ RKGDEYLNWK EFQKRGLPLN
     DH
//
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