ID A0A136JG18_9PEZI Unreviewed; 357 AA.
AC A0A136JG18;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:KXJ96058.1};
GN ORFNames=Micbo1qcDRAFT_144413 {ECO:0000313|EMBL:KXJ96058.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ96058.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-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; KQ964246; KXJ96058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JG18; -.
DR STRING; 196109.A0A136JG18; -.
DR InParanoid; A0A136JG18; -.
DR OrthoDB; 4204864at2759; -.
DR Proteomes; UP000070501; 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; cd12183; LDH_like_2; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000070501}.
FT DOMAIN 39..343
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 125..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 357 AA; 38843 MW; CB08BA40C88D4032 CRC64;
MPHLAVFSAK PYDKLFLTST RAKQLLQSSP ATSTTSTLDI VHHEFPLSVD TVSVLPKGAL
AVCVFVNDTV NADVLKALSE HGVKAVFLRC AGFNNVDLKV AEQLGLHVAN VPAYSPEAVA
EFAVALIQTL NRNTHRAYNR VREANFDLNG LLGKTLRGKT VGVIGTGRIG VAFAKIMGAG
FGCRILAFDP FESDELKKYG EYVKELDNLL PQCDIISLHC PLLDSTKHII NKKSLEKMKD
GVLLVNTSRG GLIDTKSVIA GLKSWKLGGL ALDVYEGEGG LFYSDHSGTI IHDDELMRLT
TFHNVLVCGH QAFFTEEALR EIADCTIKNM AEYIGGGECT HALVGKAQRK YSIPLRT
//
