ID I2DXT6_9BURK Unreviewed; 435 AA.
AC I2DXT6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=MYA_5114 {ECO:0000313|EMBL:AFJ89462.1};
OS Burkholderia sp. KJ006.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ89462.1, ECO:0000313|Proteomes:UP000010108};
RN [1] {ECO:0000313|EMBL:AFJ89462.1, ECO:0000313|Proteomes:UP000010108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ89462.1,
RC ECO:0000313|Proteomes:UP000010108};
RX PubMed=22843575; DOI=10.1128/JB.00821-12;
RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT Strain KJ006.";
RL J. Bacteriol. 194:4432-4433(2012).
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003516; AFJ89462.1; -; Genomic_DNA.
DR RefSeq; WP_014725528.1; NC_017922.1.
DR AlphaFoldDB; I2DXT6; -.
DR GeneID; 69523781; -.
DR KEGG; buk:MYA_5114; -.
DR PATRIC; fig|416344.3.peg.5203; -.
DR HOGENOM; CLU_042042_4_2_4; -.
DR Proteomes; UP000010108; Chromosome 3.
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}.
FT DOMAIN 336..368
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"
FT REGION 409..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 46980 MW; 24D1E53BA128F2EA CRC64;
MADLRCTIAG ITSPNPFWLA SAPPTDKAYN VNRAFEAGWG GVVWKTLGLD PHVVNVSSRY
GAVQWNGQRI AGLNNIELIT DRPLDVNLAE IAQVKRDWPD RALIVSLMVP CNERDWKWIL
PLVEDTGADA VELNFGCPHG MSERGMGAAV GQVPEYVEMV TRWVKEGTKL PCLVKLTPNI
SDIRMGSRAA YKGGADGVSL INTINSIVAV DLDQMAPMPT VDGKGTHGGY CGPAVKPIAL
NMVAEIARDP QTPNLPISGI GGISSWRDAA EFIVLGAGSV QVCTAAMHYG FRIVSDLVDG
LSNWMDDKGY ATLDDVRGRA VPNVTDWKYL NLKYDIKARI DQDRCIQCGL CHIACEDTSH
QAITATKDGV RHFEVVDAQC VGCNLCMHVC PVEQCITMER VDAGDYANWT THPNNPARAD
AGASPAQPAE PAKAA
//
