ID Q0SDK6_RHOJR Unreviewed; 294 AA.
AC Q0SDK6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Probable 2-hydroxy-3-oxopropionate reductase {ECO:0000313|EMBL:ABG94380.1};
DE EC=1.1.1.60 {ECO:0000313|EMBL:ABG94380.1};
GN OrderedLocusNames=RHA1_ro02575 {ECO:0000313|EMBL:ABG94380.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94380.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SIMILARITY: Belongs to the HIBADH-related family.
CC {ECO:0000256|ARBA:ARBA00009080}.
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DR EMBL; CP000431; ABG94380.1; -; Genomic_DNA.
DR RefSeq; WP_011595289.1; NC_008268.1.
DR AlphaFoldDB; Q0SDK6; -.
DR KEGG; rha:RHA1_ro02575; -.
DR PATRIC; fig|101510.16.peg.2606; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_0_11; -.
DR OrthoDB; 3185659at2; -.
DR Proteomes; UP000008710; 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:0046487; P:glyoxylate metabolic process; 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; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
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 InterPro; IPR006398; Tartro_sem_red.
DR NCBIfam; TIGR01505; tartro_sem_red; 1.
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.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:ABG94380.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 3..162
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 165..283
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 294 AA; 29651 MW; 5F57F4705A7CBD3D CRC64;
MSTIAFIGLG IMGSPMAVHL ANAGHQVVGY NRSPERTAAL VEAGGTAADS IAKAVAGADV
VAVMVPDSPD VQAVLTGEDG VFEHTPSGAL IIDFSSIRPD VTTALAAQAT ERGFRLIDAP
VSGGEAGAVN AALSIMVGGA PEDFESARPI LDVVGKTVVH VGPNGSGQTV KAANQLIVAG
NIQLLAEAII FLEAYGVDTA AAVEVLGGGL AGSAVLNQKA QKMLDRSFEP GFRIDLHHKD
LGIVTSAARE AGVVTPLGAV LAQLMASARA NGDGGLDHSG LLRGVERLSG RPSQ
//
