ID L5N910_9BACI Unreviewed; 428 AA.
AC L5N910;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=D479_10481 {ECO:0000313|EMBL:ELK46553.1};
OS Halobacillus sp. BAB-2008.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK46553.1, ECO:0000313|Proteomes:UP000010769};
RN [1] {ECO:0000313|EMBL:ELK46553.1, ECO:0000313|Proteomes:UP000010769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK46553.1,
RC ECO:0000313|Proteomes:UP000010769};
RX PubMed=23469348;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BAB-2008.";
RL Genome Announc. 1:E00222-12(2013).
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:ELK46553.1}.
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DR EMBL; ANPF01000041; ELK46553.1; -; Genomic_DNA.
DR RefSeq; WP_008636560.1; NZ_ANPF01000041.1.
DR AlphaFoldDB; L5N910; -.
DR PATRIC; fig|1246484.3.peg.2150; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000010769; 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; 2.
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:ELK46553.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010769}.
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; 46125 MW; B64E1DCA5417B8CA CRC64;
MADLRLDLAG IKSPNPFWLA SAPPTNSGYQ VQRAFEAGWG GAVWKTLGEP ILNVSSRFAA
VNFNGKKVAG FNNIELITDR PLEVNLKEIY ETKKKYPDHA IIASLMVEPT QEKWHEIVKR
VEDVGVDGLE LNFGCPHGMA ERGMGAASGQ VPELVEKQTM WAKEVAQTPV IVKLTPNITD
ITFTAQAAVN GGADAVSMIN TINSLAGVDI DTWDTIPNVA GKGAHGGYCG PAVKPIALNM
VAECARHPKI NVPISGMGGV SSWREAVEFM LMGATGVQVC TAAMHHGFSI VEDMIDGLNN
YLDEKNIDSV MDLVGKSVGK YSDWGNLDLN HQIVAKINND VCINCNKCHI ACEDTSHQCI
DMLKDEGGND ILRVREEDCV GCNLCSIVCP VDGAIDMVEY ANGKPPMTWN ERQTAIGAAA
ACDVDLIK
//
