ID A0A0N9HXM7_9PSEU Unreviewed; 342 AA.
AC A0A0N9HXM7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:ALG06990.1};
GN ORFNames=AOZ06_08675 {ECO:0000313|EMBL:ALG06990.1};
OS Kibdelosporangium phytohabitans.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG06990.1, ECO:0000313|Proteomes:UP000063699};
RN [1] {ECO:0000313|EMBL:ALG06990.1, ECO:0000313|Proteomes:UP000063699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG06990.1,
RC ECO:0000313|Proteomes:UP000063699};
RA Qin S., Xing K.;
RT "Genome sequencing of Kibdelosporangium phytohabitans.";
RL Submitted (JUL-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}.
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DR EMBL; CP012752; ALG06990.1; -; Genomic_DNA.
DR RefSeq; WP_054288961.1; NZ_JADBEI010000001.1.
DR AlphaFoldDB; A0A0N9HXM7; -.
DR STRING; 860235.AOZ06_08675; -.
DR KEGG; kphy:AOZ06_08675; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000063699; Chromosome.
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; cd12185; HGDH_LDH_like; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000063699}.
FT DOMAIN 49..339
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 132..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 342 AA; 37347 MW; B67EDD88B8D67FB3 CRC64;
MTYSEPAHGT RSLASSPSLT VSTVGITIYG CGRDEAVLFR EMAPRFDVTP TIVDAAVSEA
NVELARGNRC ISVGHKTHVS NATLRALGQA GVRYISTRSI GYDHIDVEYA ESIGIVVGNI
AYSPDSVADY TLMLMLMAVR NAKSIVRRVD VHDYRLSEVR GRELRDLTVG VVGTGRIGAA
VIDRLWGFGC RTLAYDINPT VSADYVPLDD LLQRSDIVTL HTPLTARTHH LLHRRRIEAM
KEGAFVINTG RGSLVDTEAL VAALETGRLG GAALDVVEGE EGVFYADYRN KPVESAYLVR
LHRLPNVFIS PHTAYYTDRA LSDTVENSIV NCLNFESGNQ HG
//