ID A0A0S6VTQ4_9BACT Unreviewed; 396 AA.
AC A0A0S6VTQ4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-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 ORFNames=U14_02059 {ECO:0000313|EMBL:GAK50818.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK50818.1};
RN [1] {ECO:0000313|EMBL:GAK50818.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(2015).
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; DF820456; GAK50818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S6VTQ4; -.
DR STRING; 1499966.U14_02059; -.
DR HOGENOM; CLU_042042_4_2_0; -.
DR Proteomes; UP000030700; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000030700}.
FT DOMAIN 332..361
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 364..393
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 396 AA; 42800 MW; 12B74751BE0ECB03 CRC64;
MELTTEFCGM PLENPFILAS APPTASIEMI ERAFQAGWGG AVTKTIKPDY MKIEDASPRF
HALKEGNRVI GFENFELVSK KDLQYWKNGI KMLRQKWPQK TLIVSIMGDC SRESWEELAK
WAEDAGAQAL ELNFSCPHGM PEKGVGAAIG QNADITRTIT AWVSQAVHIP VIVKLTPNVT
SVLPIAEAAK KGGARALAAI NTVESLTGVD LKTLTPYPKV QGWSTLGGYS GPAVKPIGLR
VISQLAQHSD LPLSAMGGIS TWSDAMEYIS LGADHVQVCT EVMVSGFGII KHLLAGTLAY
MEEMGFSCLN DFRGAALKKL TSHEALTKET KIVPEVNHQT CIKCGKCIIA CRDGGYQAIS
LKEGQISIDR ARCDGCALCM FVCPESAISH AKAAER
//
