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Database: UniProt
Entry: B2TKC9_CLOBB
LinkDB: B2TKC9_CLOBB
Original site: B2TKC9_CLOBB 
ID   B2TKC9_CLOBB            Unreviewed;       290 AA.
AC   B2TKC9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000313|EMBL:ACD22311.1};
DE            EC=1.1.1.60 {ECO:0000313|EMBL:ACD22311.1};
GN   OrderedLocusNames=CLL_A1570 {ECO:0000313|EMBL:ACD22311.1};
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD22311.1, 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; ACD22311.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2TKC9; -.
DR   KEGG; cbk:CLL_A1570; -.
DR   HOGENOM; CLU_035117_1_0_9; -.
DR   Proteomes; UP000001195; Chromosome.
DR   GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43060:SF15; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000313|EMBL:ACD22311.1}.
FT   DOMAIN          3..160
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          165..285
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   290 AA;  31700 MW;  BFBA1DCC161884CE CRC64;
     MKKIGFIGVG VMGKSMVRNL MEKGFEVSIY TRTKSKVMDV IEEGAKWCDD IKTCVKNKDF
     IITIVGYPKD VEEVYFGENG ILANAKECAC VIDMTTTSPK LSVKIYDEAK KRNIEALDAP
     VSGGDTGAKN ATLAIMVGGD LETFDKCHDV LASMGNNIIY EGKAGSGQHT KMANQIAIAG
     AISGVCEAMT YAKGANLDVQ KMLDSISTGA AGSWQMSNMA PRMLKGDFDP GFFIKHFIKD
     MKLALEESEE ASLNLEVLKK VLEMYNILDK NNLGELGTQA LIKYYEEYSK
//
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