ID A0A0X3XXE3_9ACTN Unreviewed; 322 AA.
AC A0A0X3XXE3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KUL79477.1};
GN ORFNames=ADL34_04320 {ECO:0000313|EMBL:KUL79477.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL79477.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL79477.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL79477.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
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:KUL79477.1}.
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DR EMBL; LLZN01000013; KUL79477.1; -; Genomic_DNA.
DR RefSeq; WP_062665083.1; NZ_LLZN01000013.1.
DR AlphaFoldDB; A0A0X3XXE3; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000052945; 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; IPR029753; D-isomer_DH_CS.
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.
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:UP000052945}.
FT DOMAIN 37..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..281
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 35240 MW; 15B2A3E1C1C62AFC CRC64;
MTPPVPSASR PTLLVLDADP LPRLGRLTGR VRIEHADAGT LADRLPHADV LLVWDFTSHA
VRHAWPGEGP RPRWVHTASA GVDHLMCPEL TASDTVVTNA RGVFDQPIAE YVAALVLAMA
KDLPRTLDLQ RAREWRHREG QQVAGTRACV VGSGPIGRAI ARTLKALDVT TALVGRVPRT
GIHGPEDLDR LIARADWVVA AAPLTGQTRG MFDLRRFGVM QPSARFINVG RGQLVVTEAL
AEALRKRWIA GAALDVFEDE PLGPDSPLWE VPGLLVSPHM SGDTVGWRDR LGTQFVELYE
RWEAGRPLLN VVDKQRGYVP GR
//
