ID A0A3Q7FY03_SOLLC Unreviewed; 627 AA.
AC A0A3Q7FY03;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN Name=101266918 {ECO:0000313|EnsemblPlants:Solyc03g123830.3.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc03g123830.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc03g123830.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc03g123830.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc03g123830.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc03g123830.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
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}.
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DR RefSeq; NP_001335290.1; NM_001348361.1.
DR AlphaFoldDB; A0A3Q7FY03; -.
DR SMR; A0A3Q7FY03; -.
DR STRING; 4081.A0A3Q7FY03; -.
DR PaxDb; 4081-Solyc03g123830-2-1; -.
DR EnsemblPlants; Solyc03g123830.3.1; Solyc03g123830.3.1; Solyc03g123830.3.
DR GeneID; 101266918; -.
DR Gramene; Solyc03g123830.3.1; Solyc03g123830.3.1; Solyc03g123830.3.
DR KEGG; sly:101266918; -.
DR InParanoid; A0A3Q7FY03; -.
DR OMA; NLECAYN; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000004994; Chromosome 3.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04902; ACT_3PGDH-xct; 1.
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; IPR002912; ACT_dom.
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; PTHR42938:SF46; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF01842; ACT; 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; PS51671; ACT; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU363003}; NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 555..627
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 627 AA; 66134 MW; DED79B6EBAE15077 CRC64;
MASIPSPHTA RLNSLLSSSS VNHNKPSNLS FLHASSNPSS IKLLHSVSPS ISSSSTTVIC
NVLKTVESAD ISLSRDLHGV VSTSKPTILV SEKLGEAGLD LLKSFGNVDC SYDLSPQDLC
AKISLCDALI VRSGTKVTRD VFEAAQGRLK VVGRAGVGID NVDLQAATEF GCLVVNAPTA
NTIAAAEHGI ALLTSMARNV AQSDASMKAG KWLRSKYVGV SLVGKTLAIM GFGKVGSEVA
RRAKGLGMHV IAHDPYAPAD RARAIGVDLV SFEQAISTAD FISLHMPLTP ATNKVFNDDT
FAKMKNGVRL INVARGGVID EDALVRALDS GIVAQAALDV FTVEPPPKDS KLVQHENVTV
TPHLGASTKE AQEGVAIEIA EAVVGALNGE LSATAVNAPM VPPEVLSELA PYVVLAEKVG
RLAVQLVTGG SGIQSVKVVY KSARDPDSLD TRLLRAMVTK GIIEPISDTI INLVNADFSA
KQKGLRISEE RIIVDSSPEY PVESIQVQIS NVQSRFASAL SENGNISIEG RVKYGVPHLT
RVGPFSVDVS LEGNLILCKQ VDQPGMIGKV GNILGESNVN VSFMSVGRTV KGKQAIMAIG
VDEEPDKDTQ KKIGEVSAVE EFVFLKL
//
