ID A0A3S2XU48_9RHOB Unreviewed; 433 AA.
AC A0A3S2XU48;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN Name=preA {ECO:0000313|EMBL:RVT86737.1};
GN ORFNames=DXV76_01225 {ECO:0000313|EMBL:RVT86737.1};
OS Rhodobacteraceae bacterium CCMM004.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2499834 {ECO:0000313|EMBL:RVT86737.1, ECO:0000313|Proteomes:UP000287438};
RN [1] {ECO:0000313|EMBL:RVT86737.1, ECO:0000313|Proteomes:UP000287438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM004 {ECO:0000313|EMBL:RVT86737.1,
RC ECO:0000313|Proteomes:UP000287438};
RA Zhang Z.;
RT "Salalgibacter marinus gen. nov., sp. nov., isolated from a Synechococcus
RT culture.";
RL Submitted (JAN-2019) 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:RVT86737.1}.
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DR EMBL; RZWH01000001; RVT86737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S2XU48; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000287438; 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:RVT86737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287438}.
FT DOMAIN 337..369
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 370..400
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 433 AA; 47350 MW; 777ED91D24BC351F CRC64;
MADLSTDFVG IKSPNPFWLA SAPPTDKEYN VRRAFEAGWG GVVWKTLGLD PHVVNVNGPR
YGVIHGADRR VLGLNNIELI TDRPLETNLR EIKTIKRDFP DRAMIVSLMV PCEEWAWKEI
LPKVEETGAD AIELNFGCPH GMSERGMGSA VGQVPDYIEM VTRWCKQNTR MPVLVKLTPN
ITDIRYPARA AHRGGADAVS LINTISSITS VNLDTFSPEP SIDGKGSHGG YCGPAVKPIA
LNMVAEIARD PETRGLPISG IGGITTWRDA AEFMALGSGS VQVCTAAMTY GFGIIKELTA
GLSRWMDEQG HERLSDVVGR AVPNVTDWQY LNLNYVTKAQ IDQDLCIKCG RCYAACEDTS
HQAIAIKEGR VFEVIDAECV ACNLCVDVCP VEDCITMRVL EPGELDERTG RKVAAEYANW
TTHPNNPSSQ AAE
//
