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Database: UniProt
Entry: A0A157ZLR0_9BURK
LinkDB: A0A157ZLR0_9BURK
Original site: A0A157ZLR0_9BURK 
ID   A0A157ZLR0_9BURK        Unreviewed;       318 AA.
AC   A0A157ZLR0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:SAK46462.1};
GN   ORFNames=AWB75_00929 {ECO:0000313|EMBL:SAK46462.1};
OS   Caballeronia catudaia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777136 {ECO:0000313|EMBL:SAK46462.1, ECO:0000313|Proteomes:UP000054870};
RN   [1] {ECO:0000313|EMBL:SAK46462.1, ECO:0000313|Proteomes:UP000054870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29318 {ECO:0000313|EMBL:SAK46462.1};
RA   Oliw E.H.;
RL   Submitted (JAN-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}.
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DR   EMBL; FCOF02000003; SAK46462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A157ZLR0; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000054870; 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          34..315
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          119..291
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   318 AA;  34628 MW;  7B092B05FC135E71 CRC64;
     MPTTSTPIKV AVLDDYQNVA LSMADWSPLA GRADITVFND HVAGRDALLE RLRPFDIVCA
     MRERTPFPRD IIESLPNLKL IASTGAANAS IDLDAAAARG VEVRHTGYQS TPTIEFTWAL
     ILAMMRHVPA ENRSLRDGGW QTALGAELAG KTLGLLGLGR VGSAVGVIGR AFRMNVIAWS
     QNLTRERAEE KGVELVDKDT LFNTSDVLSI HLRLSERTHH LVGANELAQM KPTSRLVNTS
     RGPLVDSAAL VDALRSGKLA GAALDVYDEE PLAANDPLRS LPNVLATPHI GYVSEELYRT
     FYGDTVRNIV EWLDARKA
//
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