ID W5N5A9_LEPOC Unreviewed; 334 AA.
AC W5N5A9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glyoxylate reductase/hydroxypyruvate reductase-like {ECO:0000313|Ensembl:ENSLOCP00000015818.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015818.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000015818.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; AHAT01001918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N5A9; -.
DR STRING; 7918.ENSLOCP00000015818; -.
DR Ensembl; ENSLOCT00000015848.1; ENSLOCP00000015818.1; ENSLOCG00000012851.1.
DR eggNOG; KOG0069; Eukaryota.
DR GeneTree; ENSGT00940000158578; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; W5N5A9; -.
DR OMA; IAWAYSD; -.
DR Proteomes; UP000018468; Linkage group LG4.
DR Bgee; ENSLOCG00000012851; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
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; IPR029753; D-isomer_DH_CS.
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:SF137; GLYOXYLATE REDUCTASE_HYDROXYPYRUVATE REDUCTASE; 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; 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:UP000018468}.
FT DOMAIN 16..331
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 123..301
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 334 AA; 35747 MW; 3978487AA58D8752 CRC64;
SYNCSQMQAA QQLVKVFVTR RIPQEGLKVL SQSGICHVQL WDSDEPVPQA ELLKGVSGAR
GLLCLLSDKI DQEVLDAAGP DLKVISTLSV GFDHLAIEDI RNRGIRVGYT PDVLTDATAE
LTVALLLATA RRIPEAVAEV KNGGWSTWKP LWMCGYGLSG STVGVIGLGR IGLAIAKRLK
PFGVKRLLYW GRTPKPEASE VEGEFVPLDA LLGESDFVVV SCALTPETQQ LCSKDFFGKM
KKTAVFVNSS RGAVVNQEDL YEALSSGQIA AAGLDVTTPE PLPPDHPLLK LKNCVILPHI
GSATYSTRGI MSVLAANNLL AGLMGGKMPS ELVL
//
