ID A0A1M3BM87_9ACTN Unreviewed; 317 AA.
AC A0A1M3BM87;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OJU85442.1};
GN ORFNames=BGO11_00360 {ECO:0000313|EMBL:OJU85442.1};
OS Solirubrobacterales bacterium 70-9.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU85442.1, ECO:0000313|Proteomes:UP000184118};
RN [1] {ECO:0000313|EMBL:OJU85442.1, ECO:0000313|Proteomes:UP000184118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-9 {ECO:0000313|EMBL:OJU85442.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJU85442.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKSH01000035; OJU85442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3BM87; -.
DR Proteomes; UP000184118; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12169; PGDH_like_1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 37..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 34026 MW; CEA460A4AF78A61C CRC64;
MKRIVLLDDY QGIALDYGGW DRVPEEWQIV ALEQHLADPD ELVEALREAE IVVAMRERTP
LPAAVLDQLP ELKLLVTTGL ANVAIDVAAA QRNGVVVCGT GIKAAPTAEL TWGLILALLR
KIPSEDAAMR FGGWQNTIGG DLEGATLGLL GFGRLGRRMA TVAQAFGMEV LAWSQNLDPE
EARAAGVEPV EKPQLFERAD IVSVHYKLSE RSRGLVGAAE LAAMKPSAYL VNTSRGPLVD
TEALVAALHA REIAGAGVDV YDAEPLAPDH PLRKTPHTVL TPHLGYVTED TYSVFFADAV
DDVLAYLGGA PVRVIEA
//
