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Database: UniProt
Entry: A0A0D0LW50_9FLAO
LinkDB: A0A0D0LW50_9FLAO
Original site: A0A0D0LW50_9FLAO 
ID   A0A0D0LW50_9FLAO        Unreviewed;       324 AA.
AC   A0A0D0LW50;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KIQ22804.1};
GN   ORFNames=RT99_06875 {ECO:0000313|EMBL:KIQ22804.1};
OS   Flavobacterium sp. MEB061.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1587524 {ECO:0000313|EMBL:KIQ22804.1, ECO:0000313|Proteomes:UP000032091};
RN   [1] {ECO:0000313|EMBL:KIQ22804.1, ECO:0000313|Proteomes:UP000032091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MEB061 {ECO:0000313|EMBL:KIQ22804.1,
RC   ECO:0000313|Proteomes:UP000032091};
RA   Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT   "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT   draft genome assemblies.";
RL   Submitted (DEC-2014) 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:KIQ22804.1}.
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DR   EMBL; JXQR01000014; KIQ22804.1; -; Genomic_DNA.
DR   RefSeq; WP_042563979.1; NZ_JXQR01000014.1.
DR   AlphaFoldDB; A0A0D0LW50; -.
DR   OrthoDB; 9777288at2; -.
DR   Proteomes; UP000032091; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          4..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          109..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   324 AA;  36108 MW;  38E7ECE758A6DC25 CRC64;
     MNVFINKNIP EAGIVLLRER GINLTINPTE NVLSRDEFIK ICQENDALLN VGTNNFDEDF
     FQQCPNLKGI ALFSVGFDAV NISSANSRKI PVGNTPDVLS RATSDIAFLL MQSVARKSFY
     NHKKIINGEW GSFNPLANLG QELYGKTLGI FGLGRIGFEM AQKCKAAFGM NIIYHNRSHN
     ENAENELNTE LVDFETLLAK SDVLSVHSNY TEENNELFNK SAFAKMKPSS IFINTARGKF
     HNEDDLFHAL TNNIIWGAGL DVTNPEPMKK DNPLLSLPNC CILPHIGSAT YEARNAMAVC
     AAQNIIALFE NKKMPFCVNE DVYF
//
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