ID A0A0A0EI33_9RHOB Unreviewed; 434 AA.
AC A0A0A0EI33;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=ATO9_08890 {ECO:0000313|EMBL:KGM48817.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM48817.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM48817.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM48817.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
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:KGM48817.1}.
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DR EMBL; AQQX01000003; KGM48817.1; -; Genomic_DNA.
DR RefSeq; WP_043747578.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EI33; -.
DR STRING; 1461694.ATO9_08890; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000030004; 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:KGM48817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030004}.
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; 47334 MW; 08065579A91F0165 CRC64;
MADLTSDFLG IKSPNPFWLA SAPPTDKEYN VRRAYEAGWG GVVWKTLGEE GPPVVNVNGP
RYGAIWGADR RLLGLNNIEL ITDRDLYRNL EEMTRVKKDY PDHALIASIM VPCEEESWKK
ILPLVEETGA DGIELNFGCP HGMSERGMGS AVGQVPEYIQ MVTEWCKKYY SKPVIVKLTP
NITDIRKPAT AAKLGGADAV SLINTINSIT HVDLDLMAPE PTIDGKGSHG GYCGPAVKPI
ALSMVSEIAR NPETQGLPIS GIGGVTTWRD AAEFMVLGCG NVQVCTAAMT YGFKVVQEMI
SGLSQWMDEK GYTSTSDFVG KAVPNVTDWQ YLNLEYVTKA KIDQDACIQC GRCYAACEDT
SHQAIAMSED RVFTVKDEEC VACNLCVNVC PVEDCITMVQ MEKGAIDPRT GREVGDYANW
TTHPNNPGAV KAAE
//
