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Database: UniProt
Entry: A0A0A0D5M2_9PROT
LinkDB: A0A0A0D5M2_9PROT
Original site: A0A0A0D5M2_9PROT 
ID   A0A0A0D5M2_9PROT        Unreviewed;       426 AA.
AC   A0A0A0D5M2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE   AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN   ORFNames=P409_12680 {ECO:0000313|EMBL:KGM34001.1};
OS   Inquilinus limosus MP06.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Inquilinus.
OX   NCBI_TaxID=1398085 {ECO:0000313|EMBL:KGM34001.1, ECO:0000313|Proteomes:UP000029995};
RN   [1] {ECO:0000313|EMBL:KGM34001.1, ECO:0000313|Proteomes:UP000029995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP06 {ECO:0000313|EMBL:KGM34001.1,
RC   ECO:0000313|Proteomes:UP000029995};
RA   Pino M., Di Conza J., Gutkind G.;
RT   "Genome sequence determination for a cystic fibrosis isolate, Inquilinus
RT   limosus.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:KGM34001.1}.
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DR   EMBL; JANX01000129; KGM34001.1; -; Genomic_DNA.
DR   RefSeq; WP_034836609.1; NZ_JANX01000129.1.
DR   AlphaFoldDB; A0A0A0D5M2; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000029995; 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:KGM34001.1}.
FT   DOMAIN          336..365
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   426 AA;  46387 MW;  15F8CCE830141864 CRC64;
     MADLSNDFLG IRSPNPYWLA SAPPTDKEYN VVRAFRAGWG GVVWKTLGED PPVVNVSSRY
     GAVSYNGTRV AGLNNIELIT DRPLDVNLRE IKQVKRDWPD RAMIVSLMVP CEEASWKAIL
     PLVEDTGADG IELNFGCPHG MSERGMGSAV GQVPEYVEMV TRWCKQHSRM PVIVKLTPNI
     TNVLAPARAA KRGGADAVSL INTIQSIVSI DLDLMAPTPT VDGLGTHGGY CGPAVKPIAL
     RMVGQIARDP ECRGMAISAI GGVSTWRDAA EFMALGATNV QVCTAAMTHG FKIVEDMATG
     LANWMDGKGY AGTRAFQGLA VPNFVEWQDL NINFKSVANI NQDACIQCGK CYIACEDTSH
     QSIFKLRTPE GARRYEINEA ECVGCNLCMH VCPVDSCITM QTVDTGRPYL NWQHHPNNPM
     RKDAAE
//
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