ID A0A151AND2_9CLOT Unreviewed; 417 AA.
AC A0A151AND2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN Name=preA_1 {ECO:0000313|EMBL:KYH29133.1};
GN ORFNames=CLCOL_12700 {ECO:0000313|EMBL:KYH29133.1};
OS Clostridium colicanis DSM 13634.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH29133.1, ECO:0000313|Proteomes:UP000075374};
RN [1] {ECO:0000313|EMBL:KYH29133.1, ECO:0000313|Proteomes:UP000075374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH29133.1,
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:KYH29133.1}.
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DR EMBL; LTBB01000005; KYH29133.1; -; Genomic_DNA.
DR RefSeq; WP_061858138.1; NZ_LTBB01000005.1.
DR AlphaFoldDB; A0A151AND2; -.
DR STRING; 1121305.CLCOL_12700; -.
DR PATRIC; fig|1121305.3.peg.1272; -.
DR Proteomes; UP000075374; 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 CDD; cd02940; DHPD_FMN; 1.
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 ECO:0000313|EMBL:KYH29133.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075374}.
FT DOMAIN 336..368
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 370..399
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 417 AA; 46147 MW; 4695170D0DE41344 CRC64;
MAYKKDLSIE FLGVKCENPF FLSSSPVCSN YDMIAKAFDA GWAGVFYKTV GIYIPDECSP
RFDITKKEGT PWTGFKNMEQ ISEKPLEVNL EYIRRLKKDY PTKVLAVSIM GSTKEEWEIL
AKKVTEAGAD MIECNFSCPQ MTSSSMGSDV GTNPALVYEY TKAVVENTHL PVIAKMTPNI
TLMQVPAKAA IEAGAKGISA INTVKSITNI DLENLTAMPV VNGKSSVSGY SGAAIKPIAL
RFISDLKHDP ELKDIPVSGI GGIETWQDCL EFLLLGCENI QVTTAVMQYG YRIVEDMISG
LSYYMEERGV EKLKDLVGLA LPNIVGADEI DRSFRIIPKI NEELCVGCGR CYISCYDGGH
QAIDWNKENR KPTINDKCVG CHLCLNVCPV YQCITPGEVR FKENREPHEV ALKTIYS
//
