ID A0A1H8U8U8_9FIRM Unreviewed; 335 AA.
AC A0A1H8U8U8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:SEO99629.1};
GN ORFNames=SAMN04490178_10883 {ECO:0000313|EMBL:SEO99629.1};
OS Propionispora vibrioides.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Propionispora.
OX NCBI_TaxID=112903 {ECO:0000313|EMBL:SEO99629.1, ECO:0000313|Proteomes:UP000198847};
RN [1] {ECO:0000313|EMBL:SEO99629.1, ECO:0000313|Proteomes:UP000198847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13305 {ECO:0000313|EMBL:SEO99629.1,
RC ECO:0000313|Proteomes:UP000198847};
RA de Groot N.N.;
RL Submitted (OCT-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; FODY01000008; SEO99629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8U8U8; -.
DR STRING; 112903.SAMN04490178_10883; -.
DR Proteomes; UP000198847; 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 GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12177; 2-Hacid_dh_12; 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; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000198847}.
FT DOMAIN 22..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 119..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 335 AA; 36607 MW; 29B79CDE3EC108C6 CRC64;
MDIHMETKIA IVNSSSFGNI FSEHIERLEA LGEVKRFTLP KDVGGKELAE HLQGYGIIIA
SVTAWYNEEF FEYKDKTLLI SRHGIGYNNI DVAAATQKGT LVTKVSSLIE REAVAENAVA
LLMTVMRKVR EASFKAKAGK WAERAKFVGN EIKGKTVGVI GFGNIGSRVG EILKNGFNAE
LIAYDPGLPT EQIKEKGATP VSLEELLGTA DIISLNACIT QDNYHLLSAR EFALLKKHVF
IVNTARGELM DETALRAALD NGTVAGIGLD VIEGEPITET HPLLAYENVV ITPHTSAYTY
ECLYGMGDKV VTDVERVLAG KVPEDVINTE LLARR
//
