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Database: UniProt
Entry: A0A091J5Z8_EGRGA
LinkDB: A0A091J5Z8_EGRGA
Original site: A0A091J5Z8_EGRGA 
ID   A0A091J5Z8_EGRGA        Unreviewed;       270 AA.
AC   A0A091J5Z8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=GRHPR reductase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=Z169_01920 {ECO:0000313|EMBL:KFP15145.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP15145.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP15145.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP15145.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; KK501480; KFP15145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091J5Z8; -.
DR   STRING; 188379.A0A091J5Z8; -.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
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; 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:SF236; 2-KETOGLUCONATE 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053119}.
FT   DOMAIN          2..270
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          60..239
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP15145.1"
FT   NON_TER         270
FT                   /evidence="ECO:0000313|EMBL:KFP15145.1"
SQ   SEQUENCE   270 AA;  29816 MW;  17E55C2819B98F42 CRC64;
     IWYHKPVINE ELLQSLPNLK IVANAGVGID NLDLNLLSSY GVKVSNTPFV VSTDTADFGM
     ALMLASSRRL MEGYQMAVSP DTEYFPANWL GAEVSGATLG IVGMGTIGYK VAERAKAFEM
     KILYHNRNQR NKEEESAVRA IYCKKIDDLL QQSDFVLLSV NLTPQTHKLI GKRELELMKP
     TATLINISRG LVVDQDALVE ALQNKVIKAA ALDVTYPEPL PRDHTLLKLK NVIITPHIGS
     ATTKTRRLMM ENMTESIQAG LTGLPIPNEV
//
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