ID A0A1I5BE31_9PSEU Unreviewed; 320 AA.
AC A0A1I5BE31;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:SFN72930.1};
GN ORFNames=SAMN05421805_106229 {ECO:0000313|EMBL:SFN72930.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFN72930.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFN72930.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFN72930.1,
RC ECO:0000313|Proteomes:UP000199398};
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|RuleBase:RU003719}.
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DR EMBL; FOUP01000006; SFN72930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5BE31; -.
DR STRING; 455193.SAMN05421805_106229; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000199398; 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; IPR029753; D-isomer_DH_CS.
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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 5..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 33880 MW; F886B152E75C1B5E CRC64;
MDKRIVVTRT VPESAVEVLR EAGAVHVCSQ DGPLSVPELH DAVRGAHAIV TMLHDRVDAE
LVAAAGPQLQ VVANVAVGYD NIDVPAVTER GVTVTNTPGV LVDATADLAF GLLLMVTRRL
GEGERLLRAR EPWTFHLGFM LGTGLQGKTL GIVGLGDIGQ AVARRARAFG MNIAYTGRRR
APVEVETELD ARHLPLEELL RTADVVSLHC PLTEQTRHLI DAAALSAMKP TAFLVNTSRG
PVVDEKALAE ALHEGRIAGA ALDVFEHEPA VEPALLELDN VAIAPHLGSA TVETRTAMAE
LAARNVAAVL RGAEPITPVG
//