ID C3XQB1_BRAFL Unreviewed; 326 AA.
AC C3XQB1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Glyoxylate reductase/hydroxypyruvate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_104160 {ECO:0000313|EMBL:EEN69724.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN69724.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN69724.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN69724.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; GG666452; EEN69724.1; -; Genomic_DNA.
DR RefSeq; XP_002613715.1; XM_002613669.1.
DR AlphaFoldDB; C3XQB1; -.
DR STRING; 7739.C3XQB1; -.
DR eggNOG; KOG0069; Eukaryota.
DR InParanoid; C3XQB1; -.
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; 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}.
FT DOMAIN 9..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 34800 MW; 6886DEF6B1812AB7 CRC64;
MSTAGKPNVY VTRRIPQKAL DLLQGECSVA QWDADDPVPR VELLKGVKGI DGLYCLLTDK
IDAEVLDAAG PGLKAVSTMS VGFDHISLPE LRKRKLPLGY TPDVLTDATA ELTVALLLTT
SRRLVEGVHE VKSGGWGTWI PLWMCGSGLS GSTVGIVGLG RIGAAVAERL KPFGVSRFLY
HGRNPKPEAA GKVGAVHVEL EELLSESDFV IATCALTPET KEMFNKTVFS KMKSSAIFIN
TSRGGVVHQE DLYEALKSGT IKAAGLDVTT PEPLPTDHPL LTLDNCVVLP HIGSATVETR
TEMAVLAARN LLAGLKGEKM PAQVQL
//
