ID A0A2A2FEK2_9EURY Unreviewed; 315 AA.
AC A0A2A2FEK2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:PAU83388.1};
GN ORFNames=CK500_11425 {ECO:0000313|EMBL:PAU83388.1};
OS Halorubrum salipaludis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=2032630 {ECO:0000313|EMBL:PAU83388.1, ECO:0000313|Proteomes:UP000218083};
RN [1] {ECO:0000313|EMBL:PAU83388.1, ECO:0000313|Proteomes:UP000218083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN019 {ECO:0000313|EMBL:PAU83388.1,
RC ECO:0000313|Proteomes:UP000218083};
RA Liu D., Zhang G.;
RT "The strain WRN001 was isolated from Binhai saline alkaline soil, Tianjin,
RT China.";
RL Submitted (AUG-2017) 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:PAU83388.1}.
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DR EMBL; NSKC01000005; PAU83388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2FEK2; -.
DR OrthoDB; 168224at2157; -.
DR Proteomes; UP000218083; 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}.
FT DOMAIN 54..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 34180 MW; E1E6E61E8F253B09 CRC64;
MSDPDIVVLR QTIHGSDGSA LAEAIRERLP DRSVALARTP TEERELLETA RIAVGLDVDE
ELLAAAENLE LFACVFAGTG HLPRDALADH GVALTNASGV HRPNISEHVI GSMITHARQW
PRAHRQQERR EWRSYETTEV YGSTVAVVGL GAIGEAVVDR LEPFDVDTTG VRYSPEKGGP
TDEVYGFDEF HDAVADAEYV VLACPLTETT RGLVDADALR TMRADAVLVN IARGPVVDTD
ALVSALRNSR IRGAALDVTD PEPLPEDHPL WGLGSVTITP HNAGHTPHYY ERVADILAEN
VGRLDGGEEL ENRVV
//
