ID A0A3P1Y0V6_9BACT Unreviewed; 321 AA.
AC A0A3P1Y0V6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:RRD63778.1};
GN ORFNames=EII26_09990 {ECO:0000313|EMBL:RRD63778.1};
OS Fretibacterium sp. OH1220_COT-178.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=2491047 {ECO:0000313|EMBL:RRD63778.1, ECO:0000313|Proteomes:UP000267192};
RN [1] {ECO:0000313|EMBL:RRD63778.1, ECO:0000313|Proteomes:UP000267192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1220_COT-178 {ECO:0000313|EMBL:RRD63778.1,
RC ECO:0000313|Proteomes:UP000267192};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRD63778.1}.
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DR EMBL; RQYL01000024; RRD63778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1Y0V6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000267192; 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; cd05301; GDH; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000267192}.
FT DOMAIN 9..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 321 AA; 35450 MW; 2AE69853C8810AD6 CRC64;
MERRGSVYVT RLLPAPIMER LREICDYEVN AEPRPATREE LLRGVRGRDA VLCLLNDRID
AEVYDAAGPQ CRLFANYGVG YNNIDVPEAH RRGVWITNTP DVLNDATADI AWALLFATAR
RVAEGDRLMR SETFSWQPEF MLGMDITGRT LGVIGAGRIG RNFARKSRGF DMKVLYAGRR
PSPEFEAETG GRFVPMDELL RESDFVSLHV PLTPETRHLI GERELGLMKR TAILINTSRG
PVVDEGALVR ALESRTIWGA GLDVFENEPD TAPGLSALDN VVMTPHVGSA TVETRVNMGL
VAVANIAAAL EGREPPNLVR A
//
