ID A0A1G9RW20_9FIRM Unreviewed; 398 AA.
AC A0A1G9RW20;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=SAMN04488502_103124 {ECO:0000313|EMBL:SDM27436.1};
OS Dendrosporobacter quercicolus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Dendrosporobacter.
OX NCBI_TaxID=146817 {ECO:0000313|EMBL:SDM27436.1, ECO:0000313|Proteomes:UP000214880};
RN [1] {ECO:0000313|EMBL:SDM27436.1, ECO:0000313|Proteomes:UP000214880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1736 {ECO:0000313|EMBL:SDM27436.1,
RC ECO:0000313|Proteomes:UP000214880};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; FNHB01000003; SDM27436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9RW20; -.
DR STRING; 146817.SAMN04488502_103124; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000214880; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000214880}.
FT DOMAIN 337..366
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 368..398
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 398 AA; 43150 MW; 3DDDE04376D862F5 CRC64;
MAATLKTNFV GIQMPNPFML ASAPPTTSAE NIARSFERGW GGAVIKTVQY SPRWIKPNVS
PRIHAVKDRN QIIGFTNFEI GSQKTLEEWA KGIAWLKQRF PEHGVLASLM HTDVLKEEEW
RETTRILDDA GADGFELNLS CSHGQAESGC GAMLGVDEEK IKMVVSWVRE ETTKPVMPKL
TALTMNVQGK GLAAKAGGAS AITAINTMNS LPGIDLDRFV PYNMVDGMSA PQGLSGKAIK
PIALGCVMRL ALATGLPISA TGGVYTWRDA AEFISLGAQT IQVCSAVMEN GYGIIDQLTG
GLLDYMERMH FASIDSFRGK ALAHITRQID LSREHKVVAS VDASRCIGCE KCIHSCRDSG
YEALRLEGKT AVCDRTQCDG CGLCAQVCPR ECISFIKK
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