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Database: UniProt
Entry: M5E6H8_MALS4
LinkDB: M5E6H8_MALS4
Original site: M5E6H8_MALS4 
ID   M5E6H8_MALS4            Unreviewed;       488 AA.
AC   M5E6H8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SHO76416.1};
GN   Name=SER3 {ECO:0000313|EMBL:SHO76416.1};
GN   ORFNames=MSYG_0754 {ECO:0000313|EMBL:SHO76416.1};
OS   Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO76416.1, ECO:0000313|Proteomes:UP000186303};
RN   [1] {ECO:0000313|Proteomes:UP000186303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX   PubMed=28100699; DOI=10.1093/nar/gkx006;
RA   Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA   Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA   Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA   Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA   Lehtioe J.;
RT   "Proteogenomics produces comprehensive and highly accurate protein-coding
RT   gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL   Nucleic Acids Res. 45:2629-2643(2017).
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; LT671821; SHO76416.1; -; Genomic_DNA.
DR   RefSeq; XP_018739319.1; XM_018885780.1.
DR   STRING; 1230383.M5E6H8; -.
DR   GeneID; 30055588; -.
DR   KEGG; msym:MSY001_0703; -.
DR   VEuPathDB; FungiDB:MSYG_0754; -.
DR   HOGENOM; CLU_019796_9_2_1; -.
DR   OMA; SKGCWEV; -.
DR   OrthoDB; 6392at2759; -.
DR   Proteomes; UP000186303; Chromosome 1.
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:UP000186303}.
FT   DOMAIN          80..399
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          186..368
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   488 AA;  53035 MW;  5DD584960A1C49BE CRC64;
     MTNQAFTRAM PSSPSMQGES PFASLLAMQQ ASEPLAQEIP VVEGQSPSQA AHGRARSVSI
     PGGANAPRIL QPFNMDSIRI LLLENVSQGA VKMLREQGFE VDFFTGAWSE EELVNKIGDY
     HAIGIRSKTR LTKRVFDAAH QLLVVGCFCI GTNQVDLEAA TKRGIAVFNS PFANSRSVAE
     LVIGELVCLA RQLADRSIEM RNGTWNKVSK GCYELRGKLL GIVGYGHIGS QLSVLAEAMG
     MHVIYHDVLP LMPLGSARQA ESLEELLSVA DFVSLHVPEL PETRGMIGAK ELAQMKPGSY
     LINNARGTVV DIPALVESLK SKHLAGCAID VYPKEPAKNG ENAFNNDLNA WASELQKQSN
     VIMTPHIGGS TEEAQRLIGI EVGNALCRYI NFGGSVGAVN FPEVNIRPIT EQETRSIRIC
     YVHHNQPGAL LAVNEIIGRH NVDKQSTDSL KEIAYLLADI SDVSESDIQD IYTRLSKTPA
     NILTRLLS
//
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