ID A0A0F4J3X0_9ACTN Unreviewed; 343 AA.
AC A0A0F4J3X0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KJY29037.1};
GN ORFNames=VR44_23910 {ECO:0000313|EMBL:KJY29037.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY29037.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY29037.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY29037.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:KJY29037.1}.
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DR EMBL; JZWV01000682; KJY29037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4J3X0; -.
DR STRING; 68223.GCA_002028425_06326; -.
DR PATRIC; fig|68223.7.peg.757; -.
DR Proteomes; UP000033551; 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; cd12167; 2-Hacid_dh_8; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 57..332
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 129..303
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 343 AA; 36268 MW; 754DADA8DDBAEF25 CRC64;
MTRPPVPPRP ATVLAMSADT RAAVLRGRAL DELLRVADVD PALLLTDFAR PGPELGGRLA
RVEVLFTGWG CPVLDAEALR RMPRLRAVVH AAGSVKGHVT DACWERGLLV SSAAAANALP
VAEYTLAAIL FSNKRVLAAA HAYRAARGPV DPLARYPAAG NYRRTVGLVG ASRTGRRVLE
LLRPFDLRVL VHDPYADPAE LASLGGEACG LDELLGRSDV VSLHAPELPG TRGLLDASRL
ALMPDGATLI NTARGSLVDT AALTRELVAG RLHAVLDHTD PEVLPAGSPL YELPNVLLTP
HVAGSLGGEL DRLASVAVEE LERYARGAGF RHPVDPGRLS YSA
//
