ID   N1QJ35_SPHMS            Unreviewed;       355 AA.
AC   N1QJ35;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:EMF10589.1};
GN   ORFNames=SEPMUDRAFT_150644 {ECO:0000313|EMBL:EMF10589.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF10589.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF10589.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF10589.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; KB456267; EMF10589.1; -; Genomic_DNA.
DR   RefSeq; XP_016758710.1; XM_016906307.1.
DR   AlphaFoldDB; N1QJ35; -.
DR   STRING; 692275.N1QJ35; -.
DR   GeneID; 27903444; -.
DR   eggNOG; KOG0067; Eukaryota.
DR   HOGENOM; CLU_019796_1_3_1; -.
DR   OMA; RGVTVCN; -.
DR   OrthoDB; 4204864at2759; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   CDD; cd05299; CtBP_dh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR043322; CtBP.
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; PTHR46029; C-TERMINAL-BINDING PROTEIN; 1.
DR   PANTHER; PTHR46029:SF7; C-TERMINAL-BINDING PROTEIN; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT   DOMAIN          63..341
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          128..297
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   355 AA;  39732 MW;  89446BD2263C576F CRC64;
     MSAEMPTFTI IQADGLYPDD SIEQQIFAPR PGQQYKLEFV STGLWPTGTP ESQPWSAIPE
     DLRKRIDGIM VLKIGFNESD LALFPKLKVI VRMGVGYDRL DRSALASRGV TVCNVPDYGT
     AEIADHAIGL MLSMRRGILL HNERQRASPP DPWMPIETPL VARLQRSTFG VFGLGRIGTA
     TALRAKAFGF KVLFYDPYLA NGVDKSLDIE RTKDIKELFR RSNVLSLHSP CTRETRNSID
     YELLSLLPKG AVLVNTSRGE VLNLDGVERC LKEDIISGAA LDVLPEEPIP EDRVHSLIQA
     YRNKEPWLEG RMVLTCHTAF YSPESFVDIR IKSCETLRDV LIDGGRSNII TPEME
//