ID W8EU13_9BACT Unreviewed; 472 AA.
AC W8EU13;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, 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=Hsw_1064 {ECO:0000313|EMBL:AHJ96659.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ96659.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ96659.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ96659.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; CP007145; AHJ96659.1; -; Genomic_DNA.
DR AlphaFoldDB; W8EU13; -.
DR STRING; 1227739.Hsw_1064; -.
DR KEGG; hsw:Hsw_1064; -.
DR PATRIC; fig|1227739.3.peg.1309; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1149; Bacteria.
DR HOGENOM; CLU_042042_4_2_10; -.
DR Proteomes; UP000019423; Chromosome.
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 ECO:0000313|EMBL:AHJ96659.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019423}.
FT DOMAIN 342..371
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 376..406
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 431..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 51710 MW; D84E6FD0EB63EBC4 CRC64;
MTVNQKRPSS MPDLSINFAG IKSPNPFWLA SAPPTNSGYQ VMKAFDAGWG GAVWKTLGVP
VVNVSSRYGS VNYRDKRMMG FNNIELISDR PLADNLREIE EVKKRFPNHA VIASLMVQSR
QEWHDIVRDV TNAGSDGIEL NFGCPHGMCE RGMGSAVGQE PAVLQTIVEW VMEVARIPVI
VKLTPNISDI TEPALAARRG GANAISLINT IQSIVGVDLD LFAPYPIVDG KGSNGGYCGP
AVKPIALNMV KNCAQHPDVQ LPISGIGGIE TWRDAVEHIL LGASSVQVCT AAMHYGFGII
REMTSGLEQY MTEKGFHTID EMVGRALPNV KHWEDLNLKY KVTASINPDK CIGCQLCYTA
CEDGAHQAIR LQPNTRIPKI IDENCVGCNL CSLVCPVEQC ITMERRDDGT QHQTWKERTA
ADDIPVTFND ERAGGRHHWV PEPSAALGKE REKTLPGKAR LYESAPETLP VE
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