ID A0A0W8BZ26_PHYNI Unreviewed; 352 AA.
AC A0A0W8BZ26;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KUF77087.1};
GN ORFNames=AM587_10005354 {ECO:0000313|EMBL:KUF77087.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF77087.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF77087.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF77087.1}.
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DR EMBL; LNFO01005647; KUF77087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8BZ26; -.
DR STRING; 4790.A0A0W8BZ26; -.
DR EnsemblProtists; KUF77087; KUF77087; AM587_10005354.
DR OMA; GIFYADC; -.
DR Proteomes; UP000052943; 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; 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:UP000052943}.
FT DOMAIN 24..351
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 134..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 352 AA; 38416 MW; BBD5DECB8E5AF823 CRC64;
MAIPDFASNT SHQENFTAAM KIAFFSTHSY DIESMERVAK EDGITPKHEL KFFTPRLDAN
SARLAEGCEG VCIFVNDVAD EAALRVLAAG GTKVMLLRCA GFDMIDLKVA KELEMPVIRV
PAYSPFAVAE HAAALMLTLN RKIHRSYNRT REQNFRLAGL LGFDLHGKTI GVVGTGKIGA
LFARIAAGFG CKVLAYDVVQ SPEALSYGVE YVSQDEIWAR SDIISLHCPL FPSTKHTINS
DSIAKMKHGV MLINTSRGGL IETKALVEGL KSGKIGAVGL DVFEGEGDYF YSDRSGAIIA
DETLARLFTF PNVIITGHQA FFTKEALDNI GHTTMANIKA YEAKEELVNE VK
//
