ID A0A426CZF2_9BACT Unreviewed; 333 AA.
AC A0A426CZF2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:RRK01376.1};
GN ORFNames=Ga0100231_000745 {ECO:0000313|EMBL:RRK01376.1};
OS Opitutaceae bacterium TAV4.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278959 {ECO:0000313|EMBL:RRK01376.1, ECO:0000313|Proteomes:UP000078325};
RN [1] {ECO:0000313|EMBL:RRK01376.1, ECO:0000313|Proteomes:UP000078325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV4 {ECO:0000313|EMBL:RRK01376.1,
RC ECO:0000313|Proteomes:UP000078325};
RA Rodrigues J., Kotak M., Lin J.;
RT "Draft genome sequences of strains TAV3 and TAV4 (Verrucomicrobial:
RT Opitutaceae) isolated from a wood-feeding termite and in silico analysis of
RT their polysaccharide-degrading enzymes.";
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:RRK01376.1}.
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DR EMBL; LXWU02000001; RRK01376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426CZF2; -.
DR STRING; 278959.Ga0100231_16360; -.
DR Proteomes; UP000078325; 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; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000078325}.
FT DOMAIN 18..114
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 333 AA; 37256 MW; 7B9BA9353CC451A1 CRC64;
MTQKLKTLFA CTIEDTDARA RIQKVTTLVE APAADTPEKI LAAATQAQAD AIIVPFTAQH
LITREVIDAL PGLRLVGSTY GGVRQNIDEL HALAKNLCVI HTGPTRIRPM AEYTLGLALT
SLTQIANYHH YMRSGEAWPR AKFGRTRILH NRKVGVIGFG WIGKGIAQLF QHFTPHISIY
SEHSTEAALR EQGFRKAPSL ASMFAECEVI ILAGGHNPKT HHMIRREHFE AMADEALFIN
IARGKMVLQS DMIDVVSKKN IHLALDVFEE EPLEADSPLR HNDRVLIAPH RANAPREFEQ
RWQFLADELE RYARGERPLT ALDPVRAAVM SES
//
