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Database: UniProt
Entry: A0A2K6EUM0_PROCO
LinkDB: A0A2K6EUM0_PROCO
Original site: A0A2K6EUM0_PROCO 
ID   A0A2K6EUM0_PROCO        Unreviewed;       317 AA.
AC   A0A2K6EUM0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glyoxylate and hydroxypyruvate reductase {ECO:0000313|Ensembl:ENSPCOP00000005430.1};
GN   Name=GRHPR {ECO:0000313|Ensembl:ENSPCOP00000005430.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000005430.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000005430.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K6EUM0; -.
DR   Ensembl; ENSPCOT00000015811.1; ENSPCOP00000005430.1; ENSPCOG00000013619.1.
DR   GeneTree; ENSGT00940000158578; -.
DR   OMA; IAWAYSD; -.
DR   Proteomes; UP000233160; Unplaced.
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; 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:UP000233160}.
FT   DOMAIN          9..315
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          125..284
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   317 AA;  34562 MW;  04FE53EA2034B368 CRC64;
     MRPVRLMKVF ITRRIPPEGI AALTRAADCE VEQWDSDEPI PDKELERGLA GAHGLLCLLS
     DRVDKRLLDA AGANLKVIST LSVGVDHLAL DEIKKRGIRV GYTPDVLTDT TAELAMSLLL
     TTCRGGWTTW KPLWMCGYGL TQSTVGIIGL GRIGQAIARR LKPFGVQRYL YTGRQPRPEE
     AAEFQAEFVS VPQLAAQSDF IVVACSLTPA TRGLCNKDFF QKMKKTAVFV NISRGDVVNQ
     DDLYQALASG QIAAAGLDVT TPEPLPTNHP LLTLKNCVIL PHIGSATYRT RNTMSLLAAN
     NLLAGLRGEP MPSELKL
//
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