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Database: UniProt
Entry: A0A0H4P101_9BACI
LinkDB: A0A0H4P101_9BACI
Original site: A0A0H4P101_9BACI 
ID   A0A0H4P101_9BACI        Unreviewed;       289 AA.
AC   A0A0H4P101;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=2-hydroxy-3-oxopropionate reductase {ECO:0000313|EMBL:AKP46655.1};
DE            EC=1.1.1.31 {ECO:0000313|EMBL:AKP46655.1};
DE            EC=1.1.1.60 {ECO:0000313|EMBL:AKP46655.1};
GN   ORFNames=BSM4216_1374 {ECO:0000313|EMBL:AKP46655.1};
OS   Bacillus smithii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP46655.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP46655.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP46655.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA   van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA   van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT   4216T.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012024; AKP46655.1; -; Genomic_DNA.
DR   RefSeq; WP_048623042.1; NZ_CP012024.1.
DR   AlphaFoldDB; A0A0H4P101; -.
DR   STRING; 1479.BSM4216_1374; -.
DR   KEGG; bsm:BSM4216_1374; -.
DR   eggNOG; COG2084; Bacteria.
DR   OrthoDB; 9786703at2; -.
DR   Proteomes; UP000036353; Chromosome.
DR   GO; GO:0008679; F:2-hydroxy-3-oxopropionate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase 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:AKP46655.1}.
FT   DOMAIN          6..162
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          167..286
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   289 AA;  31222 MW;  32930AF4D781F8C8 CRC64;
     MTKPVVGFIG TGVMGKSMAG HILADGYPLV VYNRTKEKAN ELLKNGAKWA NSPKELVKQA
     DIVFTIVGMP SDVEEVYLSE NGLIENGRSG QIFIDMTTSK PSLAVHIYQT AQSKGIYTLD
     APVSGGDIGA RNGTLAIMVG GDKEIFDRVQ DLLNVLGNNI VYQGKAGSGQ HTKMCNQIAI
     ATNMIGVCES LIYAKKAGLD PEMVLKSIST GAAGSWSLSH LAPRILKEDF EPGFYIKHFI
     KDMKIALEEA EKMNLSLPGL SLAKQMYEEL SAKGEESSGT QALIKYWAE
//
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