ID A0A1Y5RGP8_9RHOB Unreviewed; 434 AA.
AC A0A1Y5RGP8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN Name=preA {ECO:0000313|EMBL:SLN14455.1};
GN ORFNames=PSA7680_00335 {ECO:0000313|EMBL:SLN14455.1};
OS Pseudoruegeria aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=393663 {ECO:0000313|EMBL:SLN14455.1, ECO:0000313|Proteomes:UP000193409};
RN [1] {ECO:0000313|EMBL:SLN14455.1, ECO:0000313|Proteomes:UP000193409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7680 {ECO:0000313|EMBL:SLN14455.1,
RC ECO:0000313|Proteomes:UP000193409};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFQ01000002; SLN14455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RGP8; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000193409; 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 ECO:0000313|EMBL:SLN14455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193409}.
FT DOMAIN 338..370
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 371..401
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 434 AA; 46961 MW; D475C0492C5A222D CRC64;
MADLSSTFVG IKSPNPFWLA SAPPTDKEYN VRRAFEAGWG GVVWKTLGAE GPPVVNVNGP
RYGAIWGADR RLLGLNNIEL ITDRPLEVNL REIKSVKRDY PDRALVVSLM VPCEEAAWKA
ILPLVEETGA DGVELNFGCP HGMAERGMGS AVGQVPEYIE MVTRWVKQNS RMPCIVKLTP
NITDIRKPAE AAARGGADAV SLINTINSIT SVNLDEMCPE PMIDGQGSHG GYCGPAVKPI
ALNMVAEIAR NPETANIPIS GIGGVTTWRD AAEFISLGAG NVQVCTAAMT YGFKIVQEMI
SGLSQWMDEK GYASVDEVVG RAVPKVKDWQ DLNLNYVAKA SINQDDCIKC GRCFAACEDT
SHQAIAMSED RTFTVKDDEC VACNLCVNVC PVEGCITMVP MKPGEVDPRT GEVVKEEYGN
WQTHPNNPAV WAAE
//
