ID K0HXR5_9BURK Unreviewed; 437 AA.
AC K0HXR5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=C380_04145 {ECO:0000313|EMBL:AFU44550.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU44550.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU44550.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU44550.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; CP003872; AFU44550.1; -; Genomic_DNA.
DR RefSeq; WP_015012632.1; NC_018708.1.
DR AlphaFoldDB; K0HXR5; -.
DR STRING; 358220.C380_04145; -.
DR KEGG; ack:C380_04145; -.
DR PATRIC; fig|358220.3.peg.850; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_042042_4_2_4; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000006306; 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 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:AFU44550.1}.
FT DOMAIN 337..369
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 373..403
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 437 AA; 47463 MW; 34CC93B4D6FFCC93 CRC64;
MADIRSNFLG IQSPNPFWLA SAPPTDKEIN VTRAFEAGWG GVVWKTLGED PPVVNVNGPR
YSTLMSQDRR VIGLNNIELI TDRPLHTNLE EIKRVKRNWP DRAMIVSLMV PCVEESWKNI
LPLVEDTGAD GIELNFGCPH GMSERGMGAA VGQVPEYIQM VTAWCKHYSK LPVIVKLTPN
ITDVRHPARA AKAGGADAVS LINTINSIMG VDLDRMVMSP STDGWGSHGG YCGPAVKPIA
LNMVAEIARD AQTAGLPISG IGGITTWRDA AEYIALGCGT VQVCTAAMVY GFKIVQDMCD
GLSNFMDEHG YATLDDFKGQ AVPTVKDWKN LNLNHIEKAV INQDACIQCG RCHVVCEDTS
HQAITFTKEG GVRKFEINEA ECVGCNLCVS ICPVPECITM RALEPGEVDV RTGKKVTGEY
ANWTTHPNNP QRVSAAA
//
