ID A0A177HXG6_9ACTN Unreviewed; 334 AA.
AC A0A177HXG6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:OAH15622.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:OAH15622.1};
GN Name=ldhA {ECO:0000313|EMBL:OAH15622.1};
GN ORFNames=STSP_10480 {ECO:0000313|EMBL:OAH15622.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH15622.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH15622.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-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:OAH15622.1}.
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DR EMBL; LOHS01000038; OAH15622.1; -; Genomic_DNA.
DR RefSeq; WP_067272611.1; NZ_LOHS01000038.1.
DR AlphaFoldDB; A0A177HXG6; -.
DR STRING; 1716141.STSP_10480; -.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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:UP000077381}.
FT DOMAIN 8..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 334 AA; 36489 MW; C76AA7A3CA6E19A5 CRC64;
MEIIAFGVQS DEKPLIEKAF AGHHDIRCLD VFLNEDTAPI AAGHEIISTS VNADLAGRVL
EMLAAGGTRM VAQRSTGFNN IDLEVAERLG ITVARVSYYS PYSVAEFAWS LAMAINRRIV
RASTRTRDFD FRLDGLMGRD MHGRTVGVLG TGKIGEAFTR IAHGFGMNLL GWDIAENPAC
VELGMDYVEK ERLFAEADLI SLHVPLMPAT QNLIDAAALK SMKNDVILVN SSRGGLIDSQ
ALVDELRKGR FTGVGLDVYE AEAGLFFLDK SLEIVVDDTL ARLVTFPNVL VTSHQAYYTE
DAVGQIIDTT LHNVLDYKAG RRSDNVLVPS APRS
//
