ID   G3A9E0_9RALS            Unreviewed;       331 AA.
AC   G3A9E0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:CCA87895.1};
DE            EC=1.1.1.26 {ECO:0000313|EMBL:CCA87895.1};
GN   ORFNames=RALSY_mp10421 {ECO:0000313|EMBL:CCA87895.1};
OS   Ralstonia syzygii R24.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA87895.1};
RN   [1] {ECO:0000313|EMBL:CCA87895.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA87895.1};
RX   PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA   Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA   Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT   "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT   solanacearum strains form a single genomic species despite divergent
RT   lifestyles.";
RL   PLoS ONE 6:e24356-e24356(2011).
RN   [2] {ECO:0000313|EMBL:CCA87895.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=R24 {ECO:0000313|EMBL:CCA87895.1};
RA   Genoscope - CEA;
RL   Submitted (APR-2011) 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; FR854090; CCA87895.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3A9E0; -.
DR   GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; 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; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW   ECO:0000313|EMBL:CCA87895.1}.
FT   DOMAIN          6..313
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          109..289
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   331 AA;  35351 MW;  AF707D22D98E9316 CRC64;
     MRPSVLVTRA TFPDIASRLR AHFDVTDNPS DTILSPSELI ERLQGKQGVM STGSERIDSA
     LLDACPALKA VCNVGVGYNN IDVAACTARG VVVTNTPDVL TQTTADFGFA LMLATARRIT
     ESERFVRRGE WQKTGIHDQM LGSDIYGATL GILGMGRIGQ AIARRAALGF EMQVIYHNRS
     PLAAETEARA HARYVDKDTL LRESDHLVLV LPYSPEAHHT IGAAELARMK PTATLTNIAR
     GGIVDDEALA QALRRGTIAA AGLDVFEGEP RIHPGLLALS NVVLTPHIGS ASVNTRRAMA
     ALTVDNLIAA LGYGPQAGQP PTPVNPQVLQ Q
//