ID E6ZTT2_SPORE Unreviewed; 492 AA.
AC E6ZTT2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Probable 3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CBQ70639.1};
GN ORFNames=sr10307 {ECO:0000313|EMBL:CBQ70639.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ70639.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ70639.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311441; CBQ70639.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZTT2; -.
DR EnsemblFungi; CBQ70639; CBQ70639; sr10307.
DR VEuPathDB; FungiDB:sr10307; -.
DR eggNOG; KOG0068; Eukaryota.
DR HOGENOM; CLU_019796_9_1_1; -.
DR OrthoDB; 6392at2759; -.
DR Proteomes; UP000008867; Chromosome 2.
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:0006520; P:amino acid metabolic process; IEA:UniProt.
DR CDD; cd12176; PGDH_3; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
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; SSF55021; ACT-like; 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 84..404
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 188..372
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 34..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 53047 MW; 6BD06E101472000F CRC64;
MSETHGQAFH RAGFSPPANA GSFSAMMAAQ AGAQRLANGT SIHPSTSPPA SFSPPNMRAR
AASQSVPLSA PRLLTPFDTE DIRILLLENV SQGAVKMLKE QGYQVDFHTK AWSEEELIQN
IGQYHAIGIR SKTKLTAKVF RAAHKLLVVG CFCIGTNQVD LEAAAKAGVA VFNSPFANSR
SVAELVIGEM ISLSRQLGDR VNEMRAGTWN KVSKGCYEVR GKILGIVGYG HIGSQLSVLA
EAMGMQVIYY DVVPLMPLGS ARQVPTLNEL LGAADFVSLH VPELPETKNM IRTEQIKAMK
KGAYLINNAR GTVVDIPALV EGLKSGHLAG AAVDVFPKEP AASGPGTFSN ELNSWASELC
ALPNVMLTPH IGGSTEEAQR MIGIEVSDAL VRYINYGGSI GAVNFPEVDL RAITEADSRV
IRICYVHQNQ PGSLRAVNEI LGSFNVDKQH SDSYKGTAYL ISDLRVDSDN DIREIYDRIS
KTDANILTRL LT
//