ID A4J8R9_DESRM Unreviewed; 411 AA.
AC A4J8R9;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ABO51472.1};
GN OrderedLocusNames=Dred_2969 {ECO:0000313|EMBL:ABO51472.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO51472.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO51472.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO51472.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000612; ABO51472.1; -; Genomic_DNA.
DR RefSeq; WP_011879263.1; NC_009253.1.
DR AlphaFoldDB; A4J8R9; -.
DR STRING; 349161.Dred_2969; -.
DR KEGG; drm:Dred_2969; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_3_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT DOMAIN 4..96
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 110..394
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 411 AA; 45794 MW; 2288557BFBA65405 CRC64;
MDTHIIESAK RCLQCKKPRC REHCPIKTPI PQMIQMFLNG SIKDAGDMLF KNNPLSVVCS
LVCPHESQCE GNCILGNKGE PVQISSIEHY ISNYYLNSMN LRPAEPKGRQ VGIIGSGPAG
ITIAFLLALK GYRITIFEAH DKIGGVLRYG IPEFRLPKTI MDKMQQRLFE MGVKIRPNTM
IGKIISIDDL FQDGYEALFI GTGVWRPNRL RIKGESLGHV HFAIDYLKNP AVYQLGERVC
VIGAGNVAMD AARTAIRNGA REVYILYRQG REDMTARQNE IQFAEIDGVH FEFYKTPLEF
THQGVRYLET KRVEVETEQG PEQVTAEQEG FLKADSVIVA VSQLPRDIIV GNTKAIDVNG
KGLIITDEYG RTTREGVFAS GDVVTGARTV VEAARVSKNV AQAIDEYLSN K
//
