ID   A0A1M3F436_9CELL        Unreviewed;       305 AA.
AC   A0A1M3F436;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:OJV79001.1};
GN   ORFNames=BGO37_01265 {ECO:0000313|EMBL:OJV79001.1};
OS   Cellulomonas sp. 73-92.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895740 {ECO:0000313|EMBL:OJV79001.1, ECO:0000313|Proteomes:UP000184539};
RN   [1] {ECO:0000313|EMBL:OJV79001.1, ECO:0000313|Proteomes:UP000184539}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-92 {ECO:0000313|EMBL:OJV79001.1};
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|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:OJV79001.1}.
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DR   EMBL; MKTH01000018; OJV79001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3F436; -.
DR   STRING; 1895740.BGO37_01265; -.
DR   Proteomes; UP000184539; 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; cd12166; 2-Hacid_dh_7; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          27..302
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          104..271
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   305 AA;  32287 MW;  F9DDF23F545CF679 CRC64;
     MLTVTVPTPD LLDRLADLTD RVRLVLWDLV HPLPDEVAAQ VEMVVIPHYF VRPGGFDVLR
     TLPNLRLVQL PSAGFEHAVP HVPAGVTVCN GRGVHSTGTA ELAVALILAA QRGLVGSVRA
     MDAGEWHNPF GPSLADRHVL VVGAGSVAEA VVARLAPFEV AITQVARTAR GPVHGVDELP
     ALVADADVVV LTVPLDESTH HLVDADLLAR MKDGALLVNV ARGRVVDTDA LLAELVAGRL
     RAALDVTDPE PLPADHPLWH APNALITAHQ GGNTDATFPR VAALVRRQLE TLLAGDEPVN
     VVART
//