ID A7RL06_NEMVE Unreviewed; 344 AA.
AC A7RL06;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEMVEDRAFT_v1g159915 {ECO:0000313|EMBL:EDO47853.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO47853.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO47853.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; DS469517; EDO47853.1; -; Genomic_DNA.
DR RefSeq; XP_001639916.1; XM_001639866.1.
DR AlphaFoldDB; A7RL06; -.
DR STRING; 45351.A7RL06; -.
DR EnsemblMetazoa; EDO47853; EDO47853; NEMVEDRAFT_v1g159915.
DR GeneID; 5520054; -.
DR KEGG; nve:5520054; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; A7RL06; -.
DR OMA; MNVLYYN; -.
DR OrthoDB; 6392at2759; -.
DR PhylomeDB; A7RL06; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
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:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 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:UP000001593}.
FT DOMAIN 25..340
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 132..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 344 AA; 37196 MW; 15E48F8E87985C3D CRC64;
MSGILRPLVF RQNIRCLGTQ ELSKVLVTRR VPQLAMDILK TSQSCDLDVW DSDDPIPRAE
LLKRAQGKDG LYVLLTEKVD AELLDAAGPQ LRVVSTMSVG YDHVTTKELK NRNIPLGYTP
NVLTDATATL TVALLLATSR RLIEAVGEVK NGGWSTWKPM WMCGATLRGS TVGIVGLGRI
GLAVAQRLLP FGVSKIVYSG WKATPEVEKQ VNATHVDNDA LFAKSDFVLG CTALTSETQG
MFNKDAFSKM KSTAIFVNTS RGGVVNQDDL YDALKDNAIR AAGLDVTVPE PLPTDHKLLS
LPNCVILPHI GSAEDATRTE MATLAARNLL AGLRGEKMPA QADL
//
