ID A0A0B7MWP5_9FUNG Unreviewed; 308 AA.
AC A0A0B7MWP5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glyoxylate reductase {ECO:0008006|Google:ProtNLM};
GN Name=PARPA_01018.1 scaffold 1359 {ECO:0000313|EMBL:CEP07710.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP07710.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP07710.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP07710.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) 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; LN719426; CEP07710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7MWP5; -.
DR STRING; 35722.A0A0B7MWP5; -.
DR OrthoDB; 1462550at2759; -.
DR Proteomes; UP000054107; 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; 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:UP000054107}.
FT DOMAIN 3..302
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 98..275
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 308 AA; 33895 MW; 6C3568FA9C6D0AF1 CRC64;
MRRLEQQGFE LVQWPKDSSM PRETLLKDVR GAEGIICMLS DKIDKQVFDA AGPQLKVVST
MSVGYDHIDL RTAKEHGVKI GYTPDVLTDA TADLTVLLTL AAARQMKSGV RAAETGEWRE
WRPDWLCGYQ FKGKTLGVVG MGRIGQAVAS RLKAFGIDRV IYWGRNEKPG LKESLNAHFV
TFDELTSTSD FIVACCALTP ETKDVFNYDA FKNMKKNAIF VNTARGGVVD QDGLVKALQE
NLIAGAGLDV TNPEPLPTDH PLFKLDNCVI LPHIGSATIE ARETMGDMCV DNVLAALKNE
SIPFGLKY
//
