ID A0A0S8I106_9DELT Unreviewed; 411 AA.
AC A0A0S8I106;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=AMJ94_10260 {ECO:0000313|EMBL:KPK90093.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK90093.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK90093.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK90093.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK90093.1}.
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DR EMBL; LJUR01000091; KPK90093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8I106; -.
DR STRING; 1703399.AMJ94_10260; -.
DR Proteomes; UP000051218; 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; PF00037; Fer4; 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}.
FT DOMAIN 349..377
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 378..407
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 411 AA; 45622 MW; 31BB6311433140E0 CRC64;
MAKDDLFHLP VKIGNVQLRN PFIVASGPTT KRVDQLEQAE KSGWGAASIK QTFNPLPYLN
YQPRYRWLKK EKLHVFTAEY RLDMEQGLRL VEEARRKCRE LVIIANYSYV AGQDIDGWLE
AARRFEAAGA QMLELNFCCP NMSFNVDISE RAKKEVRPSS GASMGQDEDA VRWVIENTRK
VTPLPLIAKI TPEGGRISEV SKVAFEAGAA AVCSVANRLG IPAIDVWNYK KPIYNLQGQN
TMACLSGPWI KPLALRDVFE IRKLVGPGPH INGTGGVSSM EDAVQMMMCG ADSIGICTET
MISGFGFLEK WMKSLKDYMK KMGFKSARDM RDLLLPEIKP ASELTVWAGY ARVDPKKCSK
CGLCVEIGHC NAIVMTDESA SIDSKLCQGC STCIDICPKK AITMMENKRA A
//
