ID A0A0G2ZAT2_9BACT Unreviewed; 362 AA.
AC A0A0G2ZAT2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=IX53_01355 {ECO:0000313|EMBL:AKI96689.1};
OS Kosmotoga pacifica.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae;
OC Kosmotoga.
OX NCBI_TaxID=1330330 {ECO:0000313|EMBL:AKI96689.1, ECO:0000313|Proteomes:UP000035159};
RN [1] {ECO:0000313|EMBL:AKI96689.1, ECO:0000313|Proteomes:UP000035159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLHLJ1 {ECO:0000313|EMBL:AKI96689.1,
RC ECO:0000313|Proteomes:UP000035159};
RA Jiang L.J., Shao Z.Z., Jebbar M.;
RT "Complete Genome Sequence of Kosmotoga pacifica SLHLJ1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
CC {ECO:0000256|ARBA:ARBA00004725}.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; CP011232; AKI96689.1; -; Genomic_DNA.
DR RefSeq; WP_047753824.1; NZ_CP011232.1.
DR AlphaFoldDB; A0A0G2ZAT2; -.
DR STRING; 1330330.IX53_01355; -.
DR KEGG; kpf:IX53_01355; -.
DR PATRIC; fig|1330330.3.peg.275; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000035159; 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 GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.30.26.10; Dihydroorotate Dehydrogenase A, chain A, domain 2; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR023359; Dihydro_DH_chainA_dom2.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR PANTHER; PTHR48109:SF1; DIHYDROOROTATE DEHYDROGENASE (FUMARATE); 1.
DR PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; 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 Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 304..333
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 334..362
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 362 AA; 39188 MW; 1D9BCEB7C6EB7601 CRC64;
MELTVEIAGI KLKNPVLPAS GPLTGDDGKM LALEKLGVGG MVTKTISTKA AEVPRPCIIA
GNNYVMNTEL WTEYPPEKWE EEFLPRYRAK SGLPLIISLG YTVEDLEVLV PRFERFADGF
ELSTHYVADD PELMKLLIRT VKNHSKKPVF LKFDPSVPDP EGMARTIEEA GGDGIVIMNS
LGPAFPLDRK AGKSYLGSEN GFGWVSGPVI KPLSLAMVKR VAKSTSLPII GVGGISSADD
IIEFMMAGAR AVQLLSAALI RGKSLYKKIV EALPVKLQEL GVNNIEEIIG VAKDSNKEAS
FEKRTPVIDR KRCTLCGLCV DICPYFALSI ENNSVVVDTD ECFGCGLCQS RCPVKAIGGV
LI
//
