ID V4BJ65_LOTGI Unreviewed; 312 AA.
AC V4BJ65;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=LOTGIDRAFT_234402 {ECO:0000313|EMBL:ESO88814.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO88814.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO88814.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; KB202620; ESO88814.1; -; Genomic_DNA.
DR RefSeq; XP_009060485.1; XM_009062237.1.
DR AlphaFoldDB; V4BJ65; -.
DR STRING; 225164.V4BJ65; -.
DR EnsemblMetazoa; LotgiT234402; LotgiP234402; LotgiG234402.
DR GeneID; 20249526; -.
DR KEGG; lgi:LOTGIDRAFT_234402; -.
DR CTD; 20249526; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR OMA; ARGFIHD; -.
DR OrthoDB; 6392at2759; -.
DR Proteomes; UP000030746; 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: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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746}.
FT DOMAIN 6..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 34097 MW; D9FAB94D0715CCCE CRC64;
MKPKVYVTRI VHEEGLNILR EKYEVEVWNS DDVIPHDELK KHVKGISALF CTIADQIDSE
ILDAAGENLK VVATMSVGTH HINVKDCKKR GIQVTNTPDV ASDSAAELTV ALLLLTTRRC
LEGIEAVEKG EWGKWKPMWI LGTESVNRTI GIIGMGRVGF GVARRMKPFG VSRILYNDVA
PSSFAADIDA EFCSLDQLLT ESDIVCICCA LTPQTENLID KAAFHKMKSN AVLINTSRAA
VIDQEALYES LKNGVIHSAG LDVTNPEPLP KDHPLLTLDN CIILPHLGTN TSETRASMSI
NTALNIVAVL DS
//
