ID X0S1H0_9ZZZZ Unreviewed; 326 AA. AC X0S1H0; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 22-FEB-2023, entry version 21. DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722}; DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119}; DE Flags: Fragment; GN ORFNames=S01H1_07457 {ECO:0000313|EMBL:GAF69091.1}; OS marine sediment metagenome. OC unclassified sequences; metagenomes; ecological metagenomes. OX NCBI_TaxID=412755 {ECO:0000313|EMBL:GAF69091.1}; RN [1] {ECO:0000313|EMBL:GAF69091.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAF69091.1}; RX PubMed=24624126; DOI=10.3389/fmicb.2014.00080; RA Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W., RA Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F., RA Takami H.; RT "High frequency of phylogenetically diverse reductive dehalogenase- RT homologous genes in deep subseafloor sedimentary metagenomes."; RL Front. Microbiol. 5:80-80(2014). 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:GAF69091.1}. 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; BARS01003845; GAF69091.1; -; Genomic_DNA. DR AlphaFoldDB; X0S1H0; -. DR UniPathway; UPA00070; -. 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; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. DR InterPro; IPR001295; Dihydroorotate_DH_CS. 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 TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 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}. FT DOMAIN 265..293 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 296..325 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:GAF69091.1" SQ SEQUENCE 326 AA; 34224 MW; A357540ED3D2481B CRC64; DKRGMIDIEL FSELTLDRWE VEIDLIRASF PERPIIASIA GGGNPHEWQE IVRRVEPHGI NGYEMNVSCP NLGGKEKGED KAEQNTKAMA LAVGWVKEVT DLPVIVKLTP NVTDVAALAQ AAEAAGADAV TTGNSLSGLG GIDLDTFAPL PTVDGISIFG GYGGPGLKPV SLRCTAVAAQ ALQIPVIGCG GISTWQDAAE YLAVGASIVE VCTAVMWNGC RIIEKLTKGL EAYLERKGYK TPTDITGKAL SRIGSFPDLN LSIKLAASVD DSCNGCGICV EACASGGYQA ITMDSDTARV DISRCDGCGL CVGVCPQESI HLTPRQ //