ID A0A0G2B5C0_9BACT Unreviewed; 412 AA.
AC A0A0G2B5C0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KKW40544.1};
GN ORFNames=UY87_C0018G0004 {ECO:0000313|EMBL:KKW40544.1};
OS Candidatus Peribacteria bacterium GW2011_GWC2_54_8.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria.
OX NCBI_TaxID=1619063 {ECO:0000313|EMBL:KKW40544.1, ECO:0000313|Proteomes:UP000034858};
RN [1] {ECO:0000313|EMBL:KKW40544.1, ECO:0000313|Proteomes:UP000034858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW40544.1}.
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DR EMBL; LCRS01000018; KKW40544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2B5C0; -.
DR PATRIC; fig|1619063.3.peg.401; -.
DR Proteomes; UP000034858; 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; cd04901; ACT_3PGDH; 1.
DR CDD; cd12176; PGDH_3; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF55021; ACT-like; 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 16..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 121..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 412 AA; 45074 MW; 9DD0B0020D67E359 CRC64;
MSAATFSLSK EKIRFLLLEG IHNSALERLR ADGYTNVDYE TGSYDEEELS SLIGEYHFLG
IRSRALVTEK VLRKAKKLAA IGCFCIGTNQ VDLRAAKRLG IPVFNAPHSN TRSVAELVIG
ELIMLMRGIP QKTTAAHRGE WMKSPRDSRE VRGKILGIVG YGHIGSQVGV LAEGLGLRVQ
YYDIEDKLPY GNAQPVESLK DLLRTSDVVT LHVPGTELTK GMIGLKQLKE MKQGSFLINT
SRGSVVVIDA LVEALQSKHL GGASIDVFPQ EPKSNSEEFV SPLRDLENVL LTPHIGGSTM
EAQANIGKEV ADKLIQYSNN GSTRFAVNFP EVSLPPLAGN HRFMHIHENK PGMMSAINAV
FADLGINVAG QYLQIDGEIG YVITDSEPHP LSRQVSAKLR SIPGTIKSRC LY
//
