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Database: UniProt
Entry: A0A1H0I0U7_9BACL
LinkDB: A0A1H0I0U7_9BACL
Original site: A0A1H0I0U7_9BACL 
ID   A0A1H0I0U7_9BACL        Unreviewed;       321 AA.
AC   A0A1H0I0U7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:SDO24740.1};
GN   ORFNames=SAMN04487897_110114 {ECO:0000313|EMBL:SDO24740.1};
OS   Paenibacillus sp. yr247.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1761880 {ECO:0000313|EMBL:SDO24740.1, ECO:0000313|Proteomes:UP000198936};
RN   [1] {ECO:0000313|EMBL:SDO24740.1, ECO:0000313|Proteomes:UP000198936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR247 {ECO:0000313|EMBL:SDO24740.1,
RC   ECO:0000313|Proteomes:UP000198936};
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; FNIF01000010; SDO24740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0I0U7; -.
DR   STRING; 1761880.SAMN04487897_110114; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000198936; 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:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
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:UP000198936}.
FT   DOMAIN          6..320
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   321 AA;  35347 MW;  EFF3351F5BA07F66 CRC64;
     MRPKVYITRR IPDQITAMIE NHCDVRMWHE KDTTVPREIL EREITDADGL FCLLTETIDA
     QLMEMGPRLK VISNMAVGYN NIDIEAANNK GILVTNTPGI LTETTADLTF ALLMATARRI
     TEASDYLRNG KWSTWSPMLL TGQDVHGATL GIIGMGRIGE AVAKRAKGFD MKILYHNRSR
     RSGVEENFGA MYVDLKSLLR ESDFVCVLVP FSKETVNLIG KEELALMKRT SILINTSRGG
     IVNETALNDA LVEGTIWAAG LDVFSQEPIA LDHPLLSLPN VVVLPHIGSA SVNTRLGMAQ
     LAAHNLCKAL LGEIPPNLVN K
//
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