ID A0A316YL54_9BASI Unreviewed; 364 AA.
AC A0A316YL54;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=2-hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FA10DRAFT_296259 {ECO:0000313|EMBL:PWN88793.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN88793.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN88793.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN88793.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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; KZ819638; PWN88793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YL54; -.
DR STRING; 215250.A0A316YL54; -.
DR InParanoid; A0A316YL54; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000245768; 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:SF290; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT DOMAIN 85..355
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 142..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 364 AA; 38997 MW; 2EEF22A73C7AF49C CRC64;
MAPIATTTIT PQASTNREAL PKILLLDEVH LAKDELAELQ GKATVLLSKA VSRAQLMAMF
APGGEYDDIA GIYRHFGAGR SVKLTGRFDA ELVAALPKSM RFIVHNGAGY DQLDVAALSS
RNIQASNVPQ AVDDATSDIA LFLLLGALRR IPAAQLQLAQ GYFNSHFAST SARDPRGKVL
GIVGAGGIGR ALAYKASHAL GMSVIYHNRR PLTMEEEEAA AKGGMAYVPT LEGLLERADV
VSLHCPLTQE TRGLIGRAQL ARMKPSAVLI NTARGAIVKE EELAEALENS VIGGAGLDVY
EVEPAVHARL VAQKDKVLLL PHIGTLTYET QREMEAVCLR NLIAGLDTGR LKFTVPEQQS
VCFQ
//
