ID B9PNE7_TOXGV Unreviewed; 604 AA.
AC B9PNE7; A0A0F7UXX3; B6KF90; B9QK92; S7UR18; S8GQD8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582, ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143, ECO:0000256|RuleBase:RU363003};
GN ORFNames=BN1205_091750 {ECO:0000313|EMBL:CEL73348.1}, TGVEG_239820
GN {ECO:0000313|EMBL:ESS31340.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS31340.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|EMBL:ESS31340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS31340.1};
RA Paulsen I.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ESS31340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS31340.1};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEL73348.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:CEL73348.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
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 ECO:0000256|RuleBase:RU363003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216,
CC ECO:0000256|RuleBase:RU363003}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU363003}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LN714495; CEL73348.1; -; Genomic_DNA.
DR EMBL; AAYL02000189; ESS31340.1; -; Genomic_DNA.
DR AlphaFoldDB; B9PNE7; -.
DR STRING; 432359.B9PNE7; -.
DR PaxDb; 5811-TGME49_039820; -.
DR EnsemblProtists; ESS31340; ESS31340; TGVEG_239820.
DR VEuPathDB; ToxoDB:TGVEG_239820; -.
DR eggNOG; KOG0068; Eukaryota.
DR OMA; MDAKPTI; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12173; PGDH_4; 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; IPR029009; ASB_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 InterPro; IPR006236; PGDH.
DR InterPro; IPR045626; PGDH_ASB_dom.
DR NCBIfam; TIGR01327; PGDH; 1.
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 Pfam; PF19304; PGDH_inter; 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 SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 18..331
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 119..299
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 342..451
FT /note="D-3-phosphoglycerate dehydrogenase ASB"
FT /evidence="ECO:0000259|Pfam:PF19304"
FT REGION 469..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 65194 MW; 43AA0F24A9F66478 CRC64;
MAEATAQKRQ KKHGRFRVLV CDPIDQAGMD ILSSFADVDT KLKLSEEELC RVVGNYDGLM
VRSGTTVTEK IIKHGQKLKI IGRAGVGVDN VCVDAATAQG IFVVNSPNGN TMAAAELTLG
LMMALARKIP QADASVSRGE WTRSKFMGRQ LNQKTIGIIG LGQVGTHVAR VCTALGMEVL
AYDPFINEEK AKAVGCRNVA LETLLASSDF ITLHVPLLDK TRHLINADKL KLIKKDACII
NASRGGVIDE KAVAEALMAN ELAGAALDVF EEEKEFSKDN PLIQAKANGR NIILTPHIGA
STLEAQHNVA VDVALQFREA LLGGLPQSAV NLQCVRSQQL VSLVHLAEIL GRLCSKLVDE
PVETLHLKIR GSVDSANADV LLLSAAQGVL RTRCDHIVNF VNVKRIAQEH KVELVVSKEE
LTTPPQNSIL ELRVETKNSS ASVEGCCAVD GSVVLRKFLG TPIYLQMPSR RHLHSRRRPN
SEANFETSGD VASNGSSAGT EHEDADLKDA PIYMMYTIHS DTSGTLATVA QKLAGANINI
ANCHLGRRLV DDPSAPEGKT MMGLCIFHAD SEIPDEVVTT IRQLHNVKEC KVFATPQSLG
LDAI
//
