ID   A0A124IQN0_9FIRM        Unreviewed;       383 AA.
AC   A0A124IQN0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, 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=APF81_16585 {ECO:0000313|EMBL:KUO79009.1};
OS   Desulfosporosinus sp. BRH_c37.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO79009.1, ECO:0000313|Proteomes:UP000053148};
RN   [1] {ECO:0000313|EMBL:KUO79009.1, ECO:0000313|Proteomes:UP000053148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO79009.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO79009.1}.
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DR   EMBL; LOEW01000013; KUO79009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IQN0; -.
DR   Proteomes; UP000053148; 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; 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   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}.
FT   DOMAIN          327..352
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          356..383
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   383 AA;  40954 MW;  6FA7EF64E6BDCC8B CRC64;
     MANLKVNFAG VEFKNPLVLA SATPSWDGEG MKIAGLAGIG GVIPKTIGPV QDWAAHPRNG
     RFHIMRTAGR PMGMVNLELF TTKTRDAWVK EDLLVAKEGG AVIQVSILAM PNPDDTAQLV
     DEIQATGMVD LFELNVSCPM PAAGVGMHIG KSPELTFKQV KAAKSAAKIP LTVKLTPTVF
     DMVEVAKAVK EAGAEGISIS NSVRSFAGVD IETGLPLLRG YGGYSGPAIK PIVMRHLSEV
     ARAVDLPISA IGGVMSYKEI VEYIMLGATT VQTATAVMWN GYDVIGKWLG DLENWMDKKG
     YQSLDEIRGI ALPYITTTEE LAKLPPLFAR IDEDKCTNCG ICQRVCMYRA ISGNGTAYQV
     NKSDCDGCGA CVQWCPSGAV ELK
//