ID A0A372M7T1_9ACTN Unreviewed; 319 AA.
AC A0A372M7T1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=D-2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:RFU86565.1};
GN ORFNames=DY218_11650 {ECO:0000313|EMBL:RFU86565.1};
OS Streptomyces triticagri.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU86565.1, ECO:0000313|Proteomes:UP000263094};
RN [1] {ECO:0000313|EMBL:RFU86565.1, ECO:0000313|Proteomes:UP000263094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU86565.1,
RC ECO:0000313|Proteomes:UP000263094};
RA Han C.;
RT "Isolation, diversity and antifungal activity of Actinobacteria from
RT wheat.";
RL Submitted (AUG-2018) 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:RFU86565.1}.
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DR EMBL; QUAK01000064; RFU86565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372M7T1; -.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000263094; 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; cd12169; PGDH_like_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 18..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 34309 MW; 3EEED875150F64CB CRC64;
MYLRCAILDD FQSVATSSAD WDAIRDRVEV VSFPEHCPTE DELVAAVGDF DIIVTLRERV
PFPASVLDRL PRLKLLIASG MRNSVIDFAS AEANGVTVCG TQSTSTPPVE LTWALLLGLA
RGIVTESTAM RTAGPWQSTV GADLHGRRLG LLGLGRIGSR VARVGLAFGM DVRAWSEHLT
EARTGEHGVQ LASSKEELLA TSDFVSVHLV LGDRTRGLIG AAELALMKPS AYLVNTSRAA
IVDQDALLDA LRAGRIAGAG LDVFDIEPLP ADHPVRTTPR LLATPHLGYV SRNNYRTYYG
QAVENIEAFL AGSPVRRIG
//
