ID A0A125U0B9_9GAMM Unreviewed; 330 AA.
AC A0A125U0B9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:KWS02583.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:KWS02583.1};
DE EC=1.1.1.215 {ECO:0000313|EMBL:KWS02583.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:KWS02583.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:KWS02583.1};
DE EC=1.1.1.81 {ECO:0000313|EMBL:KWS02583.1};
GN ORFNames=AZ78_0127 {ECO:0000313|EMBL:KWS02583.1};
OS Lysobacter capsici AZ78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS02583.1, ECO:0000313|Proteomes:UP000023435};
RN [1] {ECO:0000313|EMBL:KWS02583.1, ECO:0000313|Proteomes:UP000023435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ78 {ECO:0000313|EMBL:KWS02583.1,
RC ECO:0000313|Proteomes:UP000023435};
RX PubMed=24762937;
RA Puopolo G., Sonego P., Engelen K., Pertot I.;
RT "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT to Plant-Pathogenic Oomycetes.";
RL Genome Announc. 2:0-0(2014).
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:KWS02583.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAJA02000001; KWS02583.1; -; Genomic_DNA.
DR RefSeq; WP_051547464.1; NZ_JAJA02000001.1.
DR AlphaFoldDB; A0A125U0B9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000023435; Unassembled WGS sequence.
DR GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016618; F:hydroxypyruvate reductase 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:KWS02583.1}.
FT DOMAIN 11..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 35269 MW; 0F350C9C2102FC42 CRC64;
MSERPRVWVS QPLFDDVIAR LDEYFEVSAT TAVTQHAPEA VAAALREADG ALVTLNDPIG
AAQIAGATRL RAIANVGVGY NNLDLPALSA AGILATNTPD VLTETTADFG WALMMATARR
ISEAERWLRE GHWQRWSFDS LLGGDVHGST LGILGMGRIG QAIARRAAGF GMRTLYHNRS
RLPEAVEREC AAGYVSFDEL LGRADHLILV LPYSPQSHHL IDAAALAKMQ AQATLTNIAR
GGIVDENALC DALEQGRLAA AGLDVYEGEP RLNPRLLEQR RVVLTPHIAS GSLATRRAMV
SLAVDNLIAA LGHGPNAGKP PSLLNAGIRD
//
