ID F2IVR6_POLGS Unreviewed; 434 AA.
AC F2IVR6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN OrderedLocusNames=SL003B_0743 {ECO:0000313|EMBL:ADZ69173.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ69173.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ69173.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; CP002568; ADZ69173.1; -; Genomic_DNA.
DR RefSeq; WP_013651493.1; NC_015259.1.
DR AlphaFoldDB; F2IVR6; -.
DR STRING; 991905.SL003B_0743; -.
DR KEGG; pgv:SL003B_0743; -.
DR PATRIC; fig|991905.3.peg.753; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_042042_4_2_5; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000008130; 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; 2.
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:UP000008130}.
FT DOMAIN 335..368
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 434 AA; 47256 MW; FFDEC88FEBEB6D49 CRC64;
MADLRSEFAG IKSPNPFWLA SAPPTDKEYN VVRAFKAGWG GVVWKTLGDP IVNVNGPRYG
AIHGKDRQLI GLNNIELITD RPLEVNLQEI KRVKRDWKDR ALVVSLMVPC EEHYWQTILK
QVEDTEADGV ELNFGCPHGM SERGMGSAVG QVPEYIEMVT RWCKQHTRMP VIVKLTPNIT
DIRKPARAAR AGGADAVSLI NTINSIVSVD LDRMCPSPTI DGKGAHGGYC GPAVKPIALN
MVAEIARDPE TAGLPISGIG GVTTWRDAAE FMALGAGNVQ VCTAAMTYGF KIVEDMIEGL
KDWMDGAGHS GVSEFVGRAV PNCSDWQHLN LNYIAKAKID QDLCIKCGRC HIACEDTSHQ
AITSMVDGVR RFEVIDAECV GCNLCVNVCP VENCITMEPM TPGSVDPRTG RTVDATYANW
TTHPRNPNAL QAAE
//
