ID A0A2D0QDL2_ICTPU Unreviewed; 347 AA.
AC A0A2D0QDL2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glyoxylate reductase/hydroxypyruvate reductase b {ECO:0000313|RefSeq:XP_017316763.1};
GN Name=grhprb {ECO:0000313|RefSeq:XP_017316763.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017316763.1};
RN [1] {ECO:0000313|RefSeq:XP_017316763.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017316763.1};
RG RefSeq;
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 RefSeq; XP_017316763.1; XM_017461274.3.
DR AlphaFoldDB; A0A2D0QDL2; -.
DR STRING; 7998.ENSIPUP00000003552; -.
DR Ensembl; ENSIPUT00000003726; ENSIPUP00000003552; ENSIPUG00000002516.
DR GeneID; 108260755; -.
DR KEGG; ipu:108260755; -.
DR CTD; 402985; -.
DR OMA; MNVLYYN; -.
DR OrthoDB; 6392at2759; -.
DR Proteomes; UP000221080; Chromosome 29.
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:SF230; GLYOXYLATE REDUCTASE_HYDROXYPYRUVATE REDUCTASE B; 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}.
FT DOMAIN 28..344
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 135..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 347 AA; 37757 MW; 8C77DFB8A9EA6280 CRC64;
MWCSRAAVRQ VALGLRGTRR TMATLPRVYV TRKVPKQGLD ILRTSAQVQI DLWDSDDPVP
RQELLQKVKG CAGLLCVLTE KIDAELLDAA GPNLKVVSTM SVGFDHLSLD ELKKRGIRIG
YTPEVLTDAV AELTVALLLA TSRRLIEATH EAKTGGWGTW RTLWLCGYEL ANSTVGILGL
GRIGVAIAER LKPFKVKKFI YTDVAPRPEL AEAIQAEYVS MDELARQSDF LAVCCALTPE
TQGVCNKKLF AKMKNTSIFI NTSRGGVVNQ EDLYTALSSG QIAGAGLDVT TPEPLPTNHP
LFTLKNCVIL PHIASASYTT RNAMSALAAN NLLAGLRGEA MPKELRL
//
