ID   R9PT57_AGAAL            Unreviewed;       424 AA.
AC   R9PT57;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=AALB_1921 {ECO:0000313|EMBL:GAD01841.1};
OS   Agarivorans albus MKT 106.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Agarivorans.
OX   NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD01841.1, ECO:0000313|Proteomes:UP000014461};
RN   [1] {ECO:0000313|EMBL:GAD01841.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT   "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT   Marine Bacterium.";
RL   Genome Announc. 1:e00367-13(2013).
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:GAD01841.1}.
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DR   EMBL; BARX01000011; GAD01841.1; -; Genomic_DNA.
DR   RefSeq; WP_016401609.1; NZ_BARX01000011.1.
DR   AlphaFoldDB; R9PT57; -.
DR   STRING; 1331007.AALB_1921; -.
DR   OrthoDB; 9808559at2; -.
DR   Proteomes; UP000014461; 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   ECO:0000313|EMBL:GAD01841.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014461}.
FT   DOMAIN          336..365
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          373..403
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   424 AA;  46328 MW;  B39E64D4277A13F4 CRC64;
     MADLSIEFAG IKSPNPFWLA SAPPTDKAYN VERAYEAGWG GVVWKTLGED PAAVNVSSRY
     SAIYDHNGEV AGFNNIELIT DRSLEVNLRE IEAVKKSWPD RALVVSLMVP CEEEAWKEIV
     KQVEQTGADG LELNFGCPHG MPERGMGAAV GQVPEYVEMV TRWCKTYSSM PVIVKLTPNI
     TDIRFSAQAA KRGGADAVSL INTINSITGI DLDQMAARPI VDGKSTHGGY CGPAVKPIAL
     NMVSEIARDP ETAGLPISGI GGIGNWRDAA EFISLGSGSV QVCTAAMIYG FRIVEEMKSG
     LSNWMDSKGY EKITDFQGLA VPNTTDWKYL NMNYKVVADI DEDKCIGCGR CYIACEDTSH
     QAINKTERAD GSVAFEVIED KCVGCNLCQI TCPVEQCIKM EQKEAEKPYM NWTQDPRNPY
     KDAS
//