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Database: UniProt
Entry: A0A101V0N5_9ACTN
LinkDB: A0A101V0N5_9ACTN
Original site: A0A101V0N5_9ACTN 
ID   A0A101V0N5_9ACTN        Unreviewed;       319 AA.
AC   A0A101V0N5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KUO20322.1};
GN   ORFNames=AQJ91_15165 {ECO:0000313|EMBL:KUO20322.1};
OS   Streptomyces dysideae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO20322.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO20322.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO20322.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT   sponge.";
RL   Submitted (OCT-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:KUO20322.1}.
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DR   EMBL; LMXB01000040; KUO20322.1; -; Genomic_DNA.
DR   RefSeq; WP_067021230.1; NZ_KQ949082.1.
DR   AlphaFoldDB; A0A101V0N5; -.
DR   STRING; 909626.AQJ91_15165; -.
DR   OrthoDB; 4324715at2; -.
DR   Proteomes; UP000053260; 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; 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.
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:UP000053260}.
FT   DOMAIN          32..309
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..278
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   319 AA;  34825 MW;  06EF2363D63C4068 CRC64;
     MTAPASVPTV LVLDAEPLPR LGRLTGRARV EHADESTLAE RLPHADVLLV WDFASHAVRH
     AWPGAGPRPR WVHTASAGVD HLMCPELTAS DTVVTNARGV FDQPIAEYVA ALVLAMGKDL
     PRTLELQGAR EWRHRESMRI AGTRACVVGS GPIGRTIART LKALDITTAL VGRTPRTGVH
     GPDDLDRLIA RADWVIAAAP LTEQTYGMFD ARRFGVMQPA ARFVNVGRGQ LVVEDALAEA
     LAKRWIAGAA LDVFEHEPLT PDSPLWRVPN LIVSPHMSGD TIGWRDALGA QFVELYERWE
     AGRPLVNVVD KQRGYVPGR
//
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