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Database: UniProt
Entry: A0A1Q5G061_9ACTN
LinkDB: A0A1Q5G061_9ACTN
Original site: A0A1Q5G061_9ACTN 
ID   A0A1Q5G061_9ACTN        Unreviewed;       303 AA.
AC   A0A1Q5G061;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=2-hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMK22_32325 {ECO:0000313|EMBL:OKJ25879.1};
OS   Streptomyces sp. CB01580.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703933 {ECO:0000313|EMBL:OKJ25879.1, ECO:0000313|Proteomes:UP000186318};
RN   [1] {ECO:0000313|EMBL:OKJ25879.1, ECO:0000313|Proteomes:UP000186318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01580 {ECO:0000313|EMBL:OKJ25879.1,
RC   ECO:0000313|Proteomes:UP000186318};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ25879.1}.
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DR   EMBL; LIXJ01000037; OKJ25879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5G061; -.
DR   STRING; 1703933.AMK22_32325; -.
DR   Proteomes; UP000186318; 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   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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186318}.
FT   DOMAIN          10..293
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          80..261
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   303 AA;  32337 MW;  BFAA4CFB59F6A0C8 CRC64;
     MAGTSLATRG LDEQLARATA LVCEVDVVDE ATLDKAPELR VVVSCRANPV NVDVEACTAR
     EIAVLTTPAR NADVTADLAF TLLLMTVRHT GRAERWLRSG AWKSEDVFEP YSTFRGLGLS
     GRTLGILGGG AIGRRMMQRA RAFGMDVVVY DPFLPSDAFG DQARIVELDE VLSTADIVTV
     HVPLAESTIG LIGDRELRLM RPDAYLVNAG RAAVVEEDAL VNALAEGRIA GAGLDVFWTE
     PVPADHPLLS LDNVTVTPHI GGASDDVVTE HSKIAERGLR AWVAGERPPA VANPAVLEPT
     TAR
//
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