ID A0A0N0SWS7_9ACTN Unreviewed; 317 AA.
AC A0A0N0SWS7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KOV57986.1};
GN ORFNames=ADL01_38620 {ECO:0000313|EMBL:KOV57986.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV57986.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV57986.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV57986.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-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:KOV57986.1}.
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DR EMBL; LGDW01000486; KOV57986.1; -; Genomic_DNA.
DR RefSeq; WP_053746727.1; NZ_LGDW01000486.1.
DR AlphaFoldDB; A0A0N0SWS7; -.
DR PATRIC; fig|1519490.3.peg.8407; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000037738; 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; cd05300; 2-Hacid_dh_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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000037738}.
FT DOMAIN 30..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..276
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 34761 MW; 2AA06C8AF1209E36 CRC64;
MPALPTLLVL DADPPPRLGR LTGRVQVVHA DESTLAARLP YADVLLVWDF ASHAVRAAWP
GEGAPRPRWV HTASAGVDHL MCPELAASDT VVTNARGVFD QAIAEYVAAL VLAMAKDLPR
TLRLQERHEW RHRESQRVAK TRACVVGSGP IGRAIAKYLK ALGVTTAIVG RTPRTGIHGP
DDLNRLMARA DWVIAAAPLT TATHRMFDTR RFGVMQPSAR FINVGRGQLV DERALAEALS
KRWIAGAALD VFEHEPLTPD SPLWDAPGLI VSPHMSGDTV GWRDELGEQF VELYERWEAG
KTLTNVVDKQ RGYVPGH
//
