ID B8E1J9_DICTD Unreviewed; 336 AA.
AC B8E1J9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:ACK41524.1};
GN OrderedLocusNames=Dtur_0195 {ECO:0000313|EMBL:ACK41524.1};
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC Dictyoglomus.
OX NCBI_TaxID=515635 {ECO:0000313|EMBL:ACK41524.1, ECO:0000313|Proteomes:UP000007719};
RN [1] {ECO:0000313|Proteomes:UP000007719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310 {ECO:0000313|Proteomes:UP000007719};
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001251; ACK41524.1; -; Genomic_DNA.
DR RefSeq; WP_012582609.1; NC_011661.1.
DR RefSeq; YP_002352138.1; NC_011661.1.
DR AlphaFoldDB; B8E1J9; -.
DR STRING; 515635.Dtur_0195; -.
DR EnsemblBacteria; ACK41524; ACK41524; Dtur_0195.
DR KEGG; dtu:Dtur_0195; -.
DR PATRIC; fig|515635.4.peg.201; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_0; -.
DR InParanoid; B8E1J9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000007719; Chromosome.
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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12177; 2-Hacid_dh_12; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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; 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:UP000007719}.
FT DOMAIN 17..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 336 AA; 37691 MW; 140C51A86CF71584 CRC64;
MYRIAVVNSS SFGKYFPEHM EKLKKIGEVE RFSLPGDLHG RELAEKLMGF NIIVASVTPF
YDEEFFEYKD ETLLITRHGI GYNNIDINSA TEKGTIVTKV PGVVEREAVA ETAVALLMTV
IRKIREASLK AREGKWEERA QFIGWEVKDK VVGIIGYGNI GSRVGEILKN GFNAKVIAYD
PNIPAEVLRE KGAEPVSFEE LLKISDIISL NASLNEKSRH MISEREFSMM KDNVIIINTA
RGELMDEEAL IRAIKSGKVA GVGLDVMKDE PPDPQNPLLH MENVVVTPHI AAYTYECLKG
MGDKVVSDIE KVVNKEIPDE IINKEVLERL PWTKKS
//
