ID A0A1I3PD67_9RHOB Unreviewed; 432 AA.
AC A0A1I3PD67;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=SAMN04488138_102290 {ECO:0000313|EMBL:SFJ19270.1};
OS Celeribacter halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=576117 {ECO:0000313|EMBL:SFJ19270.1, ECO:0000313|Proteomes:UP000183299};
RN [1] {ECO:0000313|EMBL:SFJ19270.1, ECO:0000313|Proteomes:UP000183299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8891 {ECO:0000313|EMBL:SFJ19270.1,
RC ECO:0000313|Proteomes:UP000183299};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FORY01000002; SFJ19270.1; -; Genomic_DNA.
DR RefSeq; WP_066606412.1; NZ_QKZJ01000002.1.
DR AlphaFoldDB; A0A1I3PD67; -.
DR STRING; 576117.SAMN04488138_102290; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000183299; 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:UP000183299}.
FT DOMAIN 337..369
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 432 AA; 46582 MW; 4CD57480B3B49BF0 CRC64;
MADLTSTFCG IKSPNPFWLA SAPPTDKEYN VRRAFEAGWG GVVWKTLGEE GPPVVNVNGP
RYGAIYGADR RLLGLNNIEL ITDRPLEVNL EEMTRVKKDY PDRALIASVM VPCDAESWKS
IIPRIAETGC DGFELNFGCP HGMAERGMGA AVGQVPEYIE MVTRWCKEAT DLPVIVKLTP
NITNILAPAE AALRGGADAV SLINTINSIA TVNLDLFAPE PMIDGKGTHG GYCGPAVKPI
AMNMVAEIAR NPETANLPIS GIGGVTTWRD AAEFMALGAG NVQVCTAAMT YGFKIVQEMI
SGLSQYLDEK DMALSELVGK ATPNVTDWQY LNLNHVTKAE ISQDDCIKCG RCYAACEDTS
HQAIEMSADR TFTVKDEECV ACNLCVNVCP IEGCITMKTL EKGEVDPRTG ETVGDYANWT
THPNNVAACS AE
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