ID A0A0M8TKN9_9ACTN Unreviewed; 335 AA.
AC A0A0M8TKN9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KOU61991.1};
GN ORFNames=ADK57_26055 {ECO:0000313|EMBL:KOU61991.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU61991.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
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:KOU61991.1}.
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DR EMBL; LGDG01000224; KOU61991.1; -; Genomic_DNA.
DR RefSeq; WP_053752043.1; NZ_LGDG01000224.1.
DR AlphaFoldDB; A0A0M8TKN9; -.
DR STRING; 1415546.ADK57_26055; -.
DR PATRIC; fig|1415546.3.peg.5657; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000037741; 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; 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:UP000037741}.
FT DOMAIN 21..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 120..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 335 AA; 35477 MW; 660BB85CE01D67D7 CRC64;
MPERPQALFA MTAENVPLVF PPEVLARLRE AVDIDPAVVA EDLTDATIQE TLARTEILVT
GWGCPRLDAT VLDAAPKLRA VLHSAGSVKS FATPELWQRG IAVSSAAEAN AVPVAEYTLA
MVLLAGKDVL TGRERLRTER VHPGWGLIPG IGNHGRRVGI VGASRIGRRL IELLRPFDLR
PALTDPYVDE AGAAALGVPL LGLDDLLRTS GIVTLHAPET PQTRHLIGAR ELALMPDGAV
LINTARGGLV DHDALVAELR TGRLAAILDV TDPEPLPADS LLLDLPNAFV TPHLAGSQGN
EVARLGASVV AEAKRLVSGG RLAHPVDPRA LEREA
//
