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Database: UniProt
Entry: A0A1H4AGF2_9BACI
LinkDB: A0A1H4AGF2_9BACI
Original site: A0A1H4AGF2_9BACI 
ID   A0A1H4AGF2_9BACI        Unreviewed;       320 AA.
AC   A0A1H4AGF2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:SEA34821.1};
GN   ORFNames=SAMN05421743_10485 {ECO:0000313|EMBL:SEA34821.1};
OS   Thalassobacillus cyri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Thalassobacillus.
OX   NCBI_TaxID=571932 {ECO:0000313|EMBL:SEA34821.1, ECO:0000313|Proteomes:UP000198584};
RN   [1] {ECO:0000313|EMBL:SEA34821.1, ECO:0000313|Proteomes:UP000198584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM7597 {ECO:0000313|EMBL:SEA34821.1,
RC   ECO:0000313|Proteomes:UP000198584};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNQR01000004; SEA34821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4AGF2; -.
DR   STRING; 571932.SAMN05421743_10485; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000198584; 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; 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:SF178; GLYOXYLATE REDUCTASE 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|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198584}.
FT   DOMAIN          5..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   320 AA;  35958 MW;  4332ECF3EA707A74 CRC64;
     MKPKVYITRK LNDRVVKKIE EACEVKMWEE EEVEIPREIL MKEAQEVDGL LCMLTENIDD
     ELLSCTRNLK VVSNMAVGYN NIDITAAKNR GITVTNTPGV LTETTADLTF TLLMATARRI
     VESSDYLRKG KWETWSPMQL TGQDIHGATL GIIGMGRIGE AVIKRAKGFD MNIIYHNRNR
     KYDIEEELGV VYAGLDELLR DSDFACVLTP YTSETHHLIS EREFSLMKET SVLINTARGG
     IVDEEALYHA LKKKEIWAAG LDVFEQEPLP LDHPLLALPN VVTLPHIGSA SIQTRLKMAD
     LAAENLLRAV TKQTPEHVVV
//
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