ID A0A1J4WPJ2_9BACT Unreviewed; 336 AA.
AC A0A1J4WPJ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUJ45_02260 {ECO:0000313|EMBL:OIO50827.1};
OS Parcubacteria group bacterium CG1_02_50_68.
OC Bacteria.
OX NCBI_TaxID=1805312 {ECO:0000313|EMBL:OIO50827.1, ECO:0000313|Proteomes:UP000182181};
RN [1] {ECO:0000313|EMBL:OIO50827.1, ECO:0000313|Proteomes:UP000182181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_50_68 {ECO:0000313|EMBL:OIO50827.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIO50827.1}.
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DR EMBL; MNWM01000026; OIO50827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4WPJ2; -.
DR STRING; 1805312.AUJ45_02260; -.
DR Proteomes; UP000182181; 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 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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; PS00065; D_2_HYDROXYACID_DH_1; 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}.
FT DOMAIN 41..333
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..303
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 336 AA; 36942 MW; D9A830787D6802F6 CRC64;
MRIHYFSSEG WEEEYVKAKL PNENTVFHNG SLAAFQDLSD PDAEILCTFI ESRIGEEELK
RFPALKLIAT RSTGFDHIDL VATKARGITI ANVPYYGENT VAEFTFALLL AVSRRIIDAD
ERIRETGTFS PVGLRGFDLA GKTIGVVGCG HIGVHVIRIA NGFGMKVLGF DVTRNDELAC
TLHFTYVALH ELFASSDIVT LHVPYNAHTH HLINKENIGT FKKGAYLINT SRGAVVETEA
LIEGLKNGII AGAGLDVLEE EGELNEELAL LTVPYPNADA IKIALENHYL IQHPCVIVTP
HLAFNTTEAI ERILDTTIKN IQQFAEGSPT NVVTET
//
