ID A0A024UMP7_9STRA Unreviewed; 242 AA.
AC A0A024UMP7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=D-lactate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=H310_02180 {ECO:0000313|EMBL:ETW07736.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW07736.1};
RN [1] {ECO:0000313|EMBL:ETW07736.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW07736.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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; KI913954; ETW07735.1; -; Genomic_DNA.
DR EMBL; KI913954; ETW07736.1; -; Genomic_DNA.
DR RefSeq; XP_008863828.1; XM_008865606.1.
DR RefSeq; XP_008863829.1; XM_008865607.1.
DR AlphaFoldDB; A0A024UMP7; -.
DR EnsemblFungi; H310_02180-t26_3; H310_02180-t26_3-p1; H310_02180.
DR EnsemblFungi; H310_02180-t26_4; H310_02180-t26_4-p1; H310_02180.
DR EnsemblProtists; ETW07735; ETW07735; H310_02180.
DR EnsemblProtists; ETW07736; ETW07736; H310_02180.
DR GeneID; 20079230; -.
DR VEuPathDB; FungiDB:H310_02180; -.
DR OrthoDB; 4204864at2759; -.
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 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 18..112
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..229
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 242 AA; 26797 MW; 0C95F0C490642492 CRC64;
MKISFFSVRK YDKESIIQVH ETLGLNHELQ FFSHRLKPET ALLADGSDIV VIFVNDTANE
VVIRKLVSLK VKALLLRCAG FDMVDLAAAK EVGLPVLRVP AYSPYAVAEH AAGLMMTLNR
KYHRAYNRTR EFNFNLQGLL GFDLHGKTVG VIGTGKIGVL FGKICLGFGC NVIAYDVYEN
DEAKALGMKY VSLDQLLETS DIISLHCPLF PTTKYMINEY TIRQMKKGAG VRLGGQGSTS
AM
//
