ID A0A3D5VHS3_UNCFI Unreviewed; 138 AA. AC A0A3D5VHS3; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, 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=DG577_07745 {ECO:0000313|EMBL:HCX79290.1}; OS Bacillota bacterium (Firmicutes bacterium). OC Bacteria; Bacillota. OX NCBI_TaxID=1879010 {ECO:0000313|EMBL:HCX79290.1, ECO:0000313|Proteomes:UP000261893}; RN [1] {ECO:0000313|EMBL:HCX79290.1, ECO:0000313|Proteomes:UP000261893} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA10586 {ECO:0000313|EMBL:HCX79290.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00001917}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway. CC {ECO:0000256|ARBA:ARBA00004725}. 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:HCX79290.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DPOK01000154; HCX79290.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3D5VHS3; -. DR UniPathway; UPA00070; -. DR Proteomes; UP000261893; Unassembled WGS sequence. 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 GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. 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; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH_cat. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR PANTHER; PTHR48109:SF1; DIHYDROOROTATE DEHYDROGENASE (FUMARATE); 1. DR PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1. DR Pfam; PF01180; DHO_dh; 1. DR Pfam; PF00037; Fer4; 2. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 3: Inferred from homology; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW FMN {ECO:0000256|ARBA:ARBA00022643}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}. FT DOMAIN 80..109 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 110..137 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" SQ SEQUENCE 138 AA; 15016 MW; E0D1A2ADBF4E1A30 CRC64; MDIPILGVGG IRSGREAVKM IMAGASAVQV CTAAILEGPE VYGKIARQIE QYMEERGIES LAEIQGLAHK SQRQEDLQRW QPAINPELCT ACGRCAQSCV YHAIKVGKYA VVDEERCVGC GLCITRCKFG AITPKFLD //