ID A0A151AMP1_9CLOT Unreviewed; 360 AA.
AC A0A151AMP1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN Name=preA_2 {ECO:0000313|EMBL:KYH28915.1};
GN ORFNames=CLCOL_13550 {ECO:0000313|EMBL:KYH28915.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH28915.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH28915.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH28915.1,
RC ECO:0000313|Proteomes:UP000075374};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium colicanis DSM 13634.";
RL Submitted (FEB-2016) 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:KYH28915.1}.
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DR EMBL; LTBB01000006; KYH28915.1; -; Genomic_DNA.
DR RefSeq; WP_061858216.1; NZ_LTBB01000006.1.
DR AlphaFoldDB; A0A151AMP1; -.
DR STRING; 1121305.CLCOL_13550; -.
DR PATRIC; fig|1121305.3.peg.1359; -.
DR Proteomes; UP000075374; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004159; F:dihydropyrimidine dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 2.
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 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; 2.
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 ECO:0000313|EMBL:KYH28915.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075374}.
FT DOMAIN 304..333
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 334..360
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 360 AA; 39367 MW; 467136115FB38168 CRC64;
MDLSTNIAGI KLKNPLMPAS GPLVGDYEKM MILEGFGLGC MVTKTISTIA ADVPRPCIYG
EKDMIMNAEL WSEYPPEYWL NEALPKLKRE LKVPLIVSVG YTKEDMERLI PLLDPYADAF
EISTHYVGKY LSVIGETVKT IRSHTTKPIF MKISPHIPDP VAFAKTVRDN GASGIVAINS
LGPTMKIDIK NRKVLVGNDK GEVWTSGPVI KPLALAIVNK IKSAIPDLTV IGVGGISSAE
DVVEFLLAGS NAVQMLSSAM LKGKDLYEKI IKDLPQVLEK YNFSSVEEVI KTELSKGSIK
FTPDNPVIDH EKCTKCGLCT KICPYFALSL EDKVLVDKEK CFGCSLCESR CPVHAISGVL
//
