ID H6BYD3_EXODN Unreviewed; 492 AA.
AC H6BYD3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00013143};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
GN ORFNames=HMPREF1120_05545 {ECO:0000313|EMBL:EHY57513.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57513.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY57513.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57513.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001878};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216}.
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; JH226133; EHY57513.1; -; Genomic_DNA.
DR RefSeq; XP_009157974.1; XM_009159726.1.
DR AlphaFoldDB; H6BYD3; -.
DR STRING; 858893.H6BYD3; -.
DR GeneID; 20310184; -.
DR VEuPathDB; FungiDB:HMPREF1120_05545; -.
DR eggNOG; KOG0068; Eukaryota.
DR HOGENOM; CLU_019796_9_1_1; -.
DR InParanoid; H6BYD3; -.
DR OMA; SKGCWEV; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR002912; ACT_dom.
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; PS51671; ACT; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 422..492
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 54178 MW; 794EEB47E4347BB3 CRC64;
MPASTPTGNI TIPQRSNPNG DSNATSNSLR REVSRSLSMS TSPHDTFHHR KMSMGVEGTS
PNLRRTTTGA VPKPLKPFRE QDIKILLLEN VNQTGREILQ RQGYQVEFMK SSLPEDQLIE
KIKDVHVIGI RSKTKLTSRV LAAAKNLIVI GCFCIGTNQV DLAYAASHGI CVFNSPFSNS
RSVAELVICE IIALARQLGD RSNEMHRGTW NKVSAKCWEV RGKTLGIIGY GHIGSQLSVL
AESMGMDVIY YDIVNLMGMG NARQIPTLDQ LLATADFVTC HVPELPETMN MISTHQLETM
KQGSYLINAS RGSVVDIPAL IDAMRSGKIA GAALDVYPAE PAGNGDYFNN DLNSWAEDLR
SLKNLILTPH IGGSTEEAQS AIGVEVAEAL VRYVNEGVTV GAVNMPEVTL RSLTMDEPNH
ARVIFIHQNV PGVLRRVNEI LGDHNVDKQM TDSRGDVAYL MADISNVREE EIAQLYRELE
SLKERIITRI LY
//
