ID   A0A2U0SEX6_9SPHN        Unreviewed;       296 AA.
AC   A0A2U0SEX6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:PVX29854.1};
GN   ORFNames=DD559_11360 {ECO:0000313|EMBL:PVX29854.1};
OS   Sphingomonas pokkalii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2175090 {ECO:0000313|EMBL:PVX29854.1, ECO:0000313|Proteomes:UP000245890};
RN   [1] {ECO:0000313|EMBL:PVX29854.1, ECO:0000313|Proteomes:UP000245890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L3B27 {ECO:0000313|EMBL:PVX29854.1,
RC   ECO:0000313|Proteomes:UP000245890};
RA   Menon R., Kumari S., Rameshkumar N.;
RT   "Description of Sphingomonas pokkalii sp nov, isolated from the rhizosphere
RT   of saline tolerant pokkali rice and its draft genome analysis.";
RL   Submitted (MAY-2018) 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:PVX29854.1}.
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DR   EMBL; QENQ01000001; PVX29854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U0SEX6; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000245890; 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; cd12156; HPPR; 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; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          34..293
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          96..264
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   296 AA;  30303 MW;  5FA8F878A57C05DF CRC64;
     MADLYLATTV SPTLHAALAE RFAVHDGNPP PTTRAIVGGG QMRLDAAMLE RLPALEIVAI
     HGVGYDGLDL DALRARGVRV TTTPDVLTED VADLAIGLML AVQRRIAAND ALARNGGWKA
     PLGRRASGRR IGIFGLGRIG TAIAARAAPF AGEVLYTARS AKPVPWRYLP GIAALAAESD
     VLILAAPGGA ATDGIVDARV LASLGTQGVL VNVARGSLVD EPALIAALHG GTIAGAGLDV
     FADEPHVPQA LRAMEQVVLA PHQGSATQEA RAAMAALVLA NLDAHFAGAP LPTPLL
//