ID A0A0N0XUG6_9ACTN Unreviewed; 326 AA.
AC A0A0N0XUG6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KPC60773.1};
GN ORFNames=ADL29_27775 {ECO:0000313|EMBL:KPC60773.1};
OS Streptomyces chattanoogensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66876 {ECO:0000313|EMBL:KPC60773.1, ECO:0000313|Proteomes:UP000037982};
RN [1] {ECO:0000313|Proteomes:UP000037982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5002 {ECO:0000313|Proteomes:UP000037982};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KPC60773.1}.
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DR EMBL; LGKG01000156; KPC60773.1; -; Genomic_DNA.
DR RefSeq; WP_053926315.1; NZ_LGKG01000156.1.
DR AlphaFoldDB; A0A0N0XUG6; -.
DR PATRIC; fig|66876.3.peg.6089; -.
DR Proteomes; UP000037982; 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 GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR CDD; cd05299; CtBP_dh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR043322; CtBP.
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:UP000037982}.
FT DOMAIN 16..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 34481 MW; D42C86B005961B97 CRC64;
MPRPLAVFTD LDDLDPAPGV ALLSQAGFDV RIADSAHPDA IVRAASEAVA LLVGYARVDA
DLLDRLPHVR ILATLSAGHD MIDTDAARAR GLWVCNLPDA ATEEVAVHAL ASALSLVRDL
PGADAVVRRG GWTTDLPRLP RRTSELTLGL VGMGRIASRL AELAAPIFGR IAAYDPLCPP
ERWPAAVRRM DLDALLTCSD VLSLHAPLND ATRGLISSAQ LERMPAGSFL VNVARGELVD
PTAVLEALDS GHLAGAALDV LPVEPPAPDD PVRTHPGLLL SPHSAFLSDA SRRAYVERPA
ENVIAWHRTG RPLTPVVTPA TEGIAQ
//
