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Database: UniProt
Entry: A0A0R0E2D4_9GAMM
LinkDB: A0A0R0E2D4_9GAMM
Original site: A0A0R0E2D4_9GAMM 
ID   A0A0R0E2D4_9GAMM        Unreviewed;       337 AA.
AC   A0A0R0E2D4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KRG84775.1};
GN   ORFNames=ABB34_08425 {ECO:0000313|EMBL:KRG84775.1};
OS   Stenotrophomonas daejeonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG84775.1, ECO:0000313|Proteomes:UP000050940};
RN   [1] {ECO:0000313|EMBL:KRG84775.1, ECO:0000313|Proteomes:UP000050940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG84775.1,
RC   ECO:0000313|Proteomes:UP000050940};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) 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:KRG84775.1}.
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DR   EMBL; LDJP01000048; KRG84775.1; -; Genomic_DNA.
DR   RefSeq; WP_057640868.1; NZ_LDJP01000048.1.
DR   AlphaFoldDB; A0A0R0E2D4; -.
DR   STRING; 659018.ABB34_08425; -.
DR   PATRIC; fig|659018.3.peg.1632; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000050940; 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; cd05301; GDH; 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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050940}.
FT   DOMAIN          17..313
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..291
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   337 AA;  35239 MW;  9E3DFFBA18AADCEF CRC64;
     MAERRPRVWV SQPLFDDTVA QLAAYCDVVA TPAVTAYDSA ALAAHLSGAD GALVTLNERI
     GAAEIADAPA LKVVANIGVG YNNLDLAALS AAGIVATNTP DVLTETTADL GFALLMAAAR
     RIVESDRWLR EGNWGQWSFT TMLGADLHGS TLGILGMGRI GQAIARRGHH GFGMKVLYHN
     RSRLPQETER DVGARYAGFD ELLSSADHLL LVLPYTAQNH HVIDAAALAK MKPTATLVNI
     ARGGIVDELA LAGALAGGRL ASAALDVYEN EPAVRPELLA LRNIVLTPHI GSASLATRRA
     MVQVAVDNLL AGLGIGADAG RPANALNAIA GGKTEKR
//
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