ID   R6SE22_9FIRM            Unreviewed;       398 AA.
AC   R6SE22;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=BN586_01763 {ECO:0000313|EMBL:CDC55819.1};
OS   Dorea formicigenerans CAG:28.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1263073 {ECO:0000313|EMBL:CDC55819.1, ECO:0000313|Proteomes:UP000018109};
RN   [1] {ECO:0000313|EMBL:CDC55819.1, ECO:0000313|Proteomes:UP000018109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:28 {ECO:0000313|Proteomes:UP000018109};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDC55819.1}.
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DR   EMBL; CBFN010000096; CDC55819.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6SE22; -.
DR   SMR; R6SE22; -.
DR   Proteomes; UP000018109; 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   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; PF00037; Fer4; 1.
DR   Pfam; PF12800; Fer4_4; 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   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:UP000018109}.
FT   DOMAIN          318..345
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          348..377
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   398 AA;  43607 MW;  FD5A1784E2EFBABE CRC64;
     MFDKEKLEGA DIGIDFCGYH LQSPYILSSG PLTYGSEGMI RGYKAGCGAV VTKTIRKEAA
     INPVHHMGTV NQDSLINCEK WADSDRQQWY DKEIPEAVKA GVIVIASVGH TLGEAKEIVE
     EVEKAGAHMI ELVSYTEDTL IPMLDYTKAH VKIPVICKLS GNWPDPVGTA KLCLEHGADG
     LCAIDSIGPT LKIDIKKARP ELMSGDGYGW MTGAAMRPIS MRINSEIARN TPELRNLYAS
     GGVMSADNAI EYMMAGAMGA GVCTVGILKG VNYIEKMCYD LSKRLKELGY DSVADVNRAA
     LPNFPKKEYV SKLDFHFQPF KEDGKKLCVS CGKCVNACCY EARKLAFPEM TVDQDKCRYC
     GLCVDVCPTG ALTADRAPQT AEDLELERMS KEFYESVK
//