ID A0A370GQG6_9BACI Unreviewed; 428 AA.
AC A0A370GQG6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=DFR59_102589 {ECO:0000313|EMBL:RDI45952.1};
OS Falsibacillus pallidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Falsibacillus.
OX NCBI_TaxID=493781 {ECO:0000313|EMBL:RDI45952.1, ECO:0000313|Proteomes:UP000255326};
RN [1] {ECO:0000313|EMBL:RDI45952.1, ECO:0000313|Proteomes:UP000255326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25281 {ECO:0000313|EMBL:RDI45952.1,
RC ECO:0000313|Proteomes:UP000255326};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RDI45952.1}.
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DR EMBL; QQAY01000002; RDI45952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370GQG6; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000255326; 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 Reference proteome {ECO:0000313|Proteomes:UP000255326}.
FT DOMAIN 333..365
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 370..400
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 428 AA; 46111 MW; 9E3EBE2743E41B44 CRC64;
MADLNIDLAG IKSPNPFWLA SAPPTNSGYQ VQRAFEAGWG GVVWKTLGDP IINVSSRFAA
VSFNGQRVAG FNNIELITDR PLEVNLKEIY ETKKRFPNHA IIASLMVEPK QEKWHEIVKK
VEAVGVDGLE LNFGCPHGMA ERGMGSASGQ VPELVEKQTY WAKEAAKTPV IVKLTPNITD
ITVTAEAAVR GGADAISMIN TINSLAGVDL DTWNTIPHVG GKGAHGGYCG PAVKPIALNM
VAECARNPRI NVPISGIGGI SNWKDAVEFM LMGATGVQIC TAAMHHGFRI VEDMIEGLNN
YLDEKGIPDL SGIIGKSVSK YSDWGNLDLN YQVVARINTE TCINCNKCHI ACEDTSHQCI
DMLKDGDGNA YLKVREEDCV GCNLCSIVCP VDGAIDMVEV PSGHAPMTWN QRQSALGVLE
KPKADVAK
//
