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Database: UniProt
Entry: A0A1I5BE31_9PSEU
LinkDB: A0A1I5BE31_9PSEU
Original site: A0A1I5BE31_9PSEU 
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
//
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