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Database: UniProt
Entry: A0A1Q4VBH6_9ACTN
LinkDB: A0A1Q4VBH6_9ACTN
Original site: A0A1Q4VBH6_9ACTN 
ID   A0A1Q4VBH6_9ACTN        Unreviewed;       326 AA.
AC   A0A1Q4VBH6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:OKH95205.1};
GN   ORFNames=AB852_10140 {ECO:0000313|EMBL:OKH95205.1};
OS   Streptomyces uncialis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1048205 {ECO:0000313|EMBL:OKH95205.1, ECO:0000313|Proteomes:UP000186455};
RN   [1] {ECO:0000313|EMBL:OKH95205.1, ECO:0000313|Proteomes:UP000186455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCA2648 {ECO:0000313|EMBL:OKH95205.1,
RC   ECO:0000313|Proteomes:UP000186455};
RA   Yan X., Huang T., Ge H., Shen B.;
RT   "Cloning and characterization of the uncialamcin biosynthetic gene
RT   cluster.";
RL   Submitted (JUN-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:OKH95205.1}.
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DR   EMBL; LFBV01000002; OKH95205.1; -; Genomic_DNA.
DR   RefSeq; WP_073787663.1; NZ_LFBV01000002.1.
DR   AlphaFoldDB; A0A1Q4VBH6; -.
DR   STRING; 1048205.AB852_10140; -.
DR   Proteomes; UP000186455; 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.
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:UP000186455}.
FT   DOMAIN          26..317
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   326 AA;  34950 MW;  EBAE924E81208107 CRC64;
     MSQQAATALL EPETLTALGR VCDLQALPVL DDFDTDHARA ALADTDLLVT GWGCPPLDPA
     ALEAAPGLRA IVHTAGSVRH HITDACWERG IVVSSAAAAN ALPVAEYTVA MILLSGKRVV
     ERARAYRGTR ARDQGFGVPR TDGNYRRSVG ILSASLIGRR VIDLLRPYDL EILLHDPYVT
     DTEAAALGTR PVGLVELFAN SDVVSVHTPL LPATQGLVSR SLLTSMRQDA VLVNTSRGGV
     VDQDALTELL LADRLRAVLD VTDPEVLPAD HPLWECDNAL ITPHLAGSQG NEWRRLAEVA
     VGEVARWAAG EGFAHPVLRE RLPFTA
//
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