ID F9FDF6_FUSOF Unreviewed; 283 AA.
AC F9FDF6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glyoxylate reductase 1 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=FOXB_04434 {ECO:0000313|EMBL:EGU85014.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU85014.1};
RN [1] {ECO:0000313|EMBL:EGU85014.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU85014.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU85014.1}.
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DR EMBL; AFQF01001446; EGU85014.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FDF6; -.
DR STRING; 660025.F9FDF6; -.
DR PaxDb; 5507-FOXG_07482P0; -.
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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..266
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 62..235
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGU85014.1"
SQ SEQUENCE 283 AA; 30580 MW; 4D0F89F524226C19 CRC64;
VAGNFDVEFI EHLPPSCRVI CHNGAAASSG YDQIDVKACA DRGITVTYAP DPVTNATADL
ALWLLLGSLR QLNPSLGSLR RGNFKTGIDF GRDPEGKVLG ILGMGRIGRA LKARCEPFGI
ITQYHNRSEL PPDQAAGATY VSFEKLISES DMISINIPLN PQTRHLIGAE QITKMKDGVI
IVNTARGAVI DEDALAEALD SGKIASVGLD VYEHEPMINE RLLKNERALL VPHLGTHTVE
TLTKMETCAM KNARRAVLGE PLLTPVPEHA GLQRSPSNCT RDV
//
