ID A0A1E7KAB9_9ACTN Unreviewed; 367 AA.
AC A0A1E7KAB9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OEV00868.1};
GN ORFNames=AN217_27125 {ECO:0000313|EMBL:OEV00868.1};
OS Streptomyces qinglanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943816 {ECO:0000313|EMBL:OEV00868.1, ECO:0000313|Proteomes:UP000175829};
RN [1] {ECO:0000313|EMBL:OEV00868.1, ECO:0000313|Proteomes:UP000175829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEV00868.1,
RC ECO:0000313|Proteomes:UP000175829};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(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:OEV00868.1}.
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DR EMBL; LJGV01000022; OEV00868.1; -; Genomic_DNA.
DR RefSeq; WP_069993073.1; NZ_LJGV01000022.1.
DR AlphaFoldDB; A0A1E7KAB9; -.
DR PATRIC; fig|943816.4.peg.5024; -.
DR Proteomes; UP000175829; 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; cd12171; 2-Hacid_dh_10; 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; 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; PS00671; D_2_HYDROXYACID_DH_3; 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:UP000175829}.
FT DOMAIN 65..351
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 140..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 367 AA; 38510 MW; 63CD2828058EA535 CRC64;
MTDPTAEPTR VLASGDHFIA PGLFVDALET ALRETAPGVR LEFRTQTTPW PHTPFGPVGN
VKEASGTEDE LLEALGDARV ALVQMAPFTE RVIREAPNLE LISVARGGPV NVDVAAATRA
GIPVTFAPGR NAAAAAEFAL GLMLAALRRI PASDAELKKG TWRGDYYAIE NAGIELDGTT
VGLVGYGAIG AIVARVLRAF GSTVLVADPY ADPAKAQADG VELVALEELL RRSSVVSLHA
RVTPETRHLL NADNLKLLPE GAVLVNSARG ELMDYAPLPA LLESGRLGAL ALDVYDVEPP
PAVWPLHRAP NVITTPHLAG ATRQTAGRAA AVTAAQAAAY LRGERPEFVV NPEVFETTGA
AGRGPRS
//
