ID A0A238VMK4_9RHOB Unreviewed; 435 AA.
AC A0A238VMK4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=SAMN06265370_102298 {ECO:0000313|EMBL:SNR34719.1};
OS Puniceibacterium sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1608407 {ECO:0000313|EMBL:SNR34719.1, ECO:0000313|Proteomes:UP000198417};
RN [1] {ECO:0000313|EMBL:SNR34719.1, ECO:0000313|Proteomes:UP000198417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29052 {ECO:0000313|EMBL:SNR34719.1,
RC ECO:0000313|Proteomes:UP000198417};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; FZNN01000002; SNR34719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238VMK4; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000198417; 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 Reference proteome {ECO:0000313|Proteomes:UP000198417}.
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 435 AA; 46841 MW; 509C8A6760EC1904 CRC64;
MADLTTDFVG IKSPNPFWLA SAPPTDKEYN VRRAFEAGWG GVVWKTLGEA GPPVVNVNGP
RYGAIWGADR RLLGLNNIEL ITDRPLEVNL REIKAVKRDY PDRALIVSLM VPCVEEAWKA
ILPLVEETGA DGVELNFGCP HGMSERGMGS AVGQVPEYIE MVTRWVKQNT PMPCIVKLTP
NITDVKQPAL AAMRGGADAV SLINTINSIT SVDLDLFAPE PTIDGKGAHG GYCGPAVKPI
ALNMVAEIAR TPEMAHLPIS GIGGVTTWKD AAEFMALGAG NVQVCTAAMT YGFKIVQEMI
SGLSDYMDKK GMAATSELVR KAVPNLSDWQ HLNLNYIAKA KIDQDLCISC GRCFAVCEDT
SHQAIAMSED RTFTVKDDEC VACNLCVNVC PVEDCITMEQ MAAGAIDPRT GKTVQPDYAN
WTTHPNNPGA VTAAE
//
