ID A0A1D2VH76_9ASCO Unreviewed; 374 AA.
AC A0A1D2VH76;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glyoxylate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASCRUDRAFT_145005 {ECO:0000313|EMBL:ODV60975.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV60975.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; KV454480; ODV60975.1; -; Genomic_DNA.
DR RefSeq; XP_020047282.1; XM_020189219.1.
DR AlphaFoldDB; A0A1D2VH76; -.
DR STRING; 1344418.A0A1D2VH76; -.
DR GeneID; 30962855; -.
DR InParanoid; A0A1D2VH76; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000095038; 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; cd12168; Mand_dh_like; 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; IPR029752; D-isomer_DH_CS1.
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:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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:UP000095038}.
FT DOMAIN 93..366
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 154..335
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 374 AA; 41923 MW; 1CE95A5985FC162D CRC64;
MLVKSLSLAL NFPARYSLFK HLFSTSGSSF KQKVLRIGAV GHAHEAWKDL SSQADVLQLP
LITEKYHRKE FLNDLLNNPE FKDISIITRT LDTKRQLGQF DEELLSHLPS TVKAIVHNGA
GYDQIDIKPF SQRNIQVSNV PNLVNDSTAN THIFLLLSAM RNFQIGHHKL INNKWAKVNG
APTANTPIGF DPEGLTVGIL GNGGIGRAVR DRLIPFGFKK ILYYNRNRLA PDLEKDSIYA
SFDELLKNSD IISVNLPLNS KTFHIINKET ISKMKDNVII INTARGPVID EISLIEGLKN
GKIYSCGLDV FENEPLNVNK ELLSLPNVVS IPHMGTHTFQ TMKKMEEFVV DNVKAFLKSG
KLNALVPEQK DLKF
//
