ID A0A1L7XUD6_9HELO Unreviewed; 340 AA.
AC A0A1L7XUD6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Related to glycerate-and formate-dehydrogenases {ECO:0000313|EMBL:CZR68639.1};
GN ORFNames=PAC_18538 {ECO:0000313|EMBL:CZR68639.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR68639.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR68639.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR68639.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-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; FJOG01000058; CZR68639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7XUD6; -.
DR STRING; 576137.A0A1L7XUD6; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000184330; 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; 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:UP000184330}.
FT DOMAIN 20..335
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 128..303
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 340 AA; 37118 MW; 7B7A02B52F517FE2 CRC64;
MTPSIQEKPK VLALTQPKAA GAEYLENFKS RFHLDVLSVK SRKEALPAIA EAVATTGPYS
AFIILMGTAP FEPFDGELFA PLVPDCKIIV SASAGYNEFP VDWMTEKGIW FCNTRNAVSE
PTADMALFLT LAVCRDTTRA EKSVRNGLWR NDHVPCTDPS DLTVGIIGLG AIGKHYARKV
AAFNMKVQYH NRSRASPEIE AEYNATWCPT LESLLSTSDV VSVSVPQNAE TEGMISHKEF
SQMKDGVFLI NTARGPIVDE DALITALESG KVKRAGLDVF TGEPKVNPWF LQSDKVTIQP
HLGGLTNKAA RDAERECFAN IEALFSTGRP VAPVNEIKSV
//
