ID S9S2V0_9RALS Unreviewed; 438 AA.
AC S9S2V0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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=C404_08830 {ECO:0000313|EMBL:EPX98482.1};
OS Ralstonia sp. AU12-08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1235457 {ECO:0000313|EMBL:EPX98482.1, ECO:0000313|Proteomes:UP000015343};
RN [1] {ECO:0000313|EMBL:EPX98482.1, ECO:0000313|Proteomes:UP000015343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU12-08 {ECO:0000313|EMBL:EPX98482.1,
RC ECO:0000313|Proteomes:UP000015343};
RX PubMed=24503988;
RA Zhang L., Morrison M., Rickard C.M.;
RT "Draft Genome Sequence of Ralstonia pickettii AU12-08, Isolated from an
RT Intravascular Catheter in Australia.";
RL Genome Announc. 2:e00027-14(2014).
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:EPX98482.1}.
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DR EMBL; ASZV01000013; EPX98482.1; -; Genomic_DNA.
DR RefSeq; WP_021194211.1; NZ_ASZV01000013.1.
DR AlphaFoldDB; S9S2V0; -.
DR PATRIC; fig|1235457.3.peg.1791; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR Proteomes; UP000015343; 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:EPX98482.1}.
FT DOMAIN 336..368
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 371..401
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 417..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 47554 MW; 9930CDF8A114B485 CRC64;
MADLRCTIAG IKSPNPFWLA SAPPTDKAYN VNRAFEAGWG GVVWKTLGLD PHVVNVSSRY
GAVQWNGQRI AGLNNIELIT DRPLDVNLRE IAQVKRDWPD RALIVSLMVP CNESDWKWIL
PMVEDTGADA VELNFGCPHG MSERGMGAAV GQVPEYVEMV TRWVKETTKL PCLVKLTPNI
TDIRLGSRAA YKGGADGVSL INTINSIVAV DLDQMAPMPT VDGKGTHGGY CGPAVKPIAL
NMVAEIARDT QTPNLPISGI GGISNWRDAA EFIVLGAGSV QVCTAAMHYG FRIVQDMADG
LANWMDEKGY ATLDDIRGRA VPNVTDWKYL NLKYDIKARI DQDRCIQCGL CHIACEDTSH
QAITREKDGK RHFEVIDAEC VGCNLCMHVC PVEQCITMER VDAGDYANWT THPNNPARVV
ASAPDAGATE PAPAAKAA
//
