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Database: UniProt
Entry: B2TRJ9_CLOBB
LinkDB: B2TRJ9_CLOBB
Original site: B2TRJ9_CLOBB 
ID   B2TRJ9_CLOBB            Unreviewed;       423 AA.
AC   B2TRJ9; U4P6U7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Hypothetical oxidoreductase YeiT {ECO:0000313|EMBL:ACD23036.1};
GN   OrderedLocusNames=CLL_A2318 {ECO:0000313|EMBL:ACD23036.1};
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD23036.1, ECO:0000313|Proteomes:UP000001195};
RN   [1] {ECO:0000313|Proteomes:UP000001195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001056; ACD23036.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2TRJ9; -.
DR   KEGG; cbk:CLL_A2318; -.
DR   PATRIC; fig|935198.13.peg.2275; -.
DR   HOGENOM; CLU_000422_3_3_9; -.
DR   Proteomes; UP000001195; 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; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          11..111
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          127..401
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   423 AA;  46381 MW;  04615AD78044A460 CRC64;
     MYKNNKMKKN NEELISPVFA IEESSRCLLC YDAPCSQACP IGTNPAKFIR SLRFRNLKGA
     VETIRENNIL GGVCARVCPT KKYCEGACSR TSIDKPIEIA KLQQYLTDYE NVLGLEILNK
     VEINKEKVAI VGSGPSGLAA ATKLAQLGYN VTVFEKRKKL GGWLTYGIPE ERLSQAVVDN
     EIEYIKNIGV EFKTNVNIGK DVTIDSLRKE GYKAFLIACG MQKSKEVKIN GSDLEGVING
     TDFLAEVKST GEYKLGNKVI VIGGGDVAID CAMTAKNLGS EDVKIVYRRT IEKMPAERKS
     IQEVIDLNIP IFTGIKPGEI IGENGKVSRF KGTGMFDDSN LDIPTENVIF AIGQEQEEVS
     SIANLDLNNK GIIETKEYAT NIDGVFACGD IVEGDKTVVY ALKLGKEAAE KVDQYLNEKE
     GAR
//
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