ID A0A0T5X7R3_9BACT Unreviewed; 363 AA.
AC A0A0T5X7R3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=HMPREF1705_03474 {ECO:0000313|EMBL:KRT34525.1};
OS Acetomicrobium hydrogeniformans ATCC BAA-1850.
OC Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC Acetomicrobium.
OX NCBI_TaxID=592015 {ECO:0000313|EMBL:KRT34525.1, ECO:0000313|Proteomes:UP000005273};
RN [1] {ECO:0000313|EMBL:KRT34525.1, ECO:0000313|Proteomes:UP000005273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1850 {ECO:0000313|Proteomes:UP000005273};
RA Gruening B.A., Erxleben A., Flemming S., Lucas X., Doering K.,
RA Weitnauer G., Bechthold A., Guenther S.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:KRT34525.1}.
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DR EMBL; ACJX03000001; KRT34525.1; -; Genomic_DNA.
DR RefSeq; WP_009200597.1; NZ_ACJX03000001.1.
DR AlphaFoldDB; A0A0T5X7R3; -.
DR STRING; 592015.HMPREF1705_03474; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1149; Bacteria.
DR OrthoDB; 9794954at2; -.
DR UniPathway; UPA00070; -.
DR Proteomes; UP000005273; 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 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 Gene3D; 2.30.26.10; Dihydroorotate Dehydrogenase A, chain A, domain 2; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR023359; Dihydro_DH_chainA_dom2.
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; 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.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; 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 Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 306..335
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 336..363
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 363 AA; 38909 MW; 8F3814C868D441D4 CRC64;
MSNLKVKIAG MEFENPLIIA AGPPSRNYET IKRMVEGGAG GVVTKTISAK AADVPRPCMA
AFKESFINTE LWSEHSPEHW LKEEYDKIYE LPVPIIVGLG YTAEELTDLI PKTEPFADAF
ELSTHYVGRD LTPVLNTVTA ARKATKKPII VKVSPGVPDL AELGKKLEEV GVDALAAINS
VGPALRIDLK TGLPYMGSDT GYGWVSGPAI KGIALRHVFE LSHAVSIPVI GVGGVSSGED
VIEMFMAGAS AVQICTQAIL EGPKAFKRIA QETSKWLDEH GYSSLEEIKG LTAKKWSSRK
EPLVKVTPSV NEEKCIGCRR CEESCVYYAI NVGSSGKAGV TTDACFGCGL CYTRCPVGAI
TLS
//
