ID A0A2N1J8W4_9BASI Unreviewed; 478 AA.
AC A0A2N1J8W4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phosphoglycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MVES_002843 {ECO:0000313|EMBL:PKI82989.1};
OS Malassezia vespertilionis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI82989.1, ECO:0000313|Proteomes:UP000232875};
RN [1] {ECO:0000313|EMBL:PKI82989.1, ECO:0000313|Proteomes:UP000232875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI82989.1,
RC ECO:0000313|Proteomes:UP000232875};
RA Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA Weller T.J., Blehert D.S.;
RT "A novel species of cold-tolerant Malassezia isolated from bats.";
RL Submitted (OCT-2017) 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; KZ454992; PKI82989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1J8W4; -.
DR STRING; 2020962.A0A2N1J8W4; -.
DR OrthoDB; 6392at2759; -.
DR Proteomes; UP000232875; 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 GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000232875}.
FT DOMAIN 70..390
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 174..358
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 478 AA; 52734 MW; 2D3735632940E6FF CRC64;
MTNQSFTRIA HSPNSRQADG VSFSTLSAMQ QALSHEPLAT SPPNQRRLSF PGGMQHPRLL
QPFDREEIRI LLLENVSQGA VEMLREQGYE IDFHTNAWSE DELVAKISEY HAIGIRSKTQ
LTRRVFEAAE KLLVVGCFCI GTNQVDLQTA AHHGIPVFNS PFANSRSVAE LVIGEMVALS
RQFVDRTLEL KSGTWNKVSK GCFELRGKLL GIVGYGHIGS QLSVLAESMG MRVIYYDVMP
LMPLGSARQA DTLDELLSEA DFISLHVPGL PETRGMIGSR EFAMMKPGAY FLNNSRGTVV
DIPAFIDALE SKHLAGGAVD VFPREPAKNG AKTFNDELNE WTSALQRQSN VILTPHIGGS
TEEAQSMIGI EVGNALCRYL NFGGSIGAVN FPEVNLRHIT EQEVRSIRIC YVHHNQPGAL
LAVNEIIGEH NVDKQSTDSM KDIAYLLADI SLVSDAEIRD IYTRLSKTRA CILTRLLS
//
