(data stored in SCRATCH zone)

SWISSPROT: B6HFP1_PENRW

ID   B6HFP1_PENRW            Unreviewed;       463 AA.
AC   B6HFP1;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU366013};
DE            EC=1.1.1.399 {ECO:0000256|RuleBase:RU366013};
DE            EC=1.1.1.95 {ECO:0000256|RuleBase:RU366013};
GN   ORFNames=Pc20g00530 {ECO:0000313|EMBL:CAP85382.1}, PCH_Pc20g00530
GN   {ECO:0000313|EMBL:CAP85382.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85382.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85382.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-
CC       glycerate to 3-phosphonooxypyruvate, the first step of the
CC       phosphorylated L-serine biosynthesis pathway. Also catalyzes the
CC       reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
CC       {ECO:0000256|RuleBase:RU366013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.399;
CC         Evidence={ECO:0000256|RuleBase:RU366013};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000256|RuleBase:RU366013};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000256|RuleBase:RU366013}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AM920435; CAP85382.1; -; Genomic_DNA.
DR   RefSeq; XP_002562615.1; XM_002562569.1.
DR   STRING; 1108849.XP_002562615.1; -.
DR   EnsemblFungi; CAP85382; CAP85382; PCH_Pc20g00530.
DR   GeneID; 8307710; -.
DR   KEGG; pcs:Pc20g00530; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136696; -.
DR   KO; K00058; -.
DR   OMA; YHAIGIR; -.
DR   OrthoDB; 911009at2759; -.
DR   BioCyc; PCHR:PC20G00530-MONOMER; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-UniRule.
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   InterPro; IPR029015; PGDH_2.
DR   PANTHER; PTHR10996:SF165; PTHR10996:SF165; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 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;
DR   PRODOM; B6HFP1.
DR   SWISS-2DPAGE; B6HFP1.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU366013};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   NAD {ECO:0000256|RuleBase:RU366013};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Serine biosynthesis {ECO:0000256|RuleBase:RU366013}.
FT   DOMAIN      393    463       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   463 AA;  50487 MW;  D40411467A4A6BCD CRC64;
     MSNARDIRPR QDDASLLATS PSASFNSPSS HSSAFNRTVP VNAKPLKPFA TEDIKVLLLE
     NVNQTGREIL SQQGYQVEFL KSSLPEDQLI EKIRDVHVIG IRSKTKLTAR VLKEAKNLIV
     IGCFCIGTNQ VDLQYAADQG IAVFNSPFSN SRSVAELVIG EMVMLARQLG DRSSEMHAGT
     WNKVSNGCWE IRGKTLGIIG YGHIGAQLSV LAEAMGMSVI YYDVLNIMSL GTARQVEALD
     DLLAEADFIT CHVPELPETK GMIGQKQFEK MKKGSYLINA SRGTVVDIPA LIDAMRSGKV
     AGAALDVYPN EPAGNGDYFN NDLNSWGADL RSLKNLILTP HIGGSTEEAQ KAIGVEVAQA
     LVRYANEGST LGAVNLPEVV LRSLTMDEPD HARVIYIHKN IPGVLRKVNE IIGDHNVDKQ
     MTDSRGDVAY LMADISNVDA ATIKELYTSL ESLPSRIMTR VLY
//

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