ID A0A0S8I498_9DELT Unreviewed; 382 AA.
AC A0A0S8I498;
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};
DE Flags: Fragment;
GN ORFNames=AMJ94_07680 {ECO:0000313|EMBL:KPK91228.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK91228.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK91228.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK91228.1};
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:KPK91228.1}.
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DR EMBL; LJUR01000056; KPK91228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8I498; -.
DR STRING; 1703399.AMJ94_07680; -.
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; 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}.
FT DOMAIN 324..352
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 353..382
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPK91228.1"
SQ SEQUENCE 382 AA; 41728 MW; 40D523B960D3D110 CRC64;
ILKNPIIIAS GTPTYGPANV KKCIRSDAAA FVTKTLCYTE WLRQQPRPRW HVEYPEAIEE
GGYFSLYSTE RLNPSPPEEY ARKKMKEYAR EAHDFDVKVI ASIAGTDGET WAKLTDLATE
NGADMIELNL QCPHVEKGQP TGMVAGRNSE LCHSILQQVK GRTSLPVIGK VLGEGVDPIK
IATRMIDGGA DAVVLTGRYQ GLYLDIETEK PILWGGMGGY GGFWQASITR KWLVRASEAD
LKAPVIGGAG IGSYEDVISY ILCGACSVQV CTAVIVYGHK IIKRWLRQVS GWMDAKGYSS
IADFSGRAAK NIIPPSQIPG DTPYASRIDP GACQKCLRCM EACPYEAISV ADKKLVVNLE
KCDGCRLCAA LCPHGAVEFF ER
//
