ID B4FWI4_MAIZE Unreviewed; 624 AA.
AC B4FWI4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN Name=100280688 {ECO:0000313|EnsemblPlants:Zm00001eb040890_P001};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF86477.1};
RN [1] {ECO:0000313|EMBL:ACF86477.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACF86477.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [2] {ECO:0000313|EnsemblPlants:Zm00001eb040890_P001, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb040890_P001,
RC ECO:0000313|Proteomes:UP000007305};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb040890_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb040890_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) 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 EMBL; BT041472; ACF86477.1; -; mRNA.
DR RefSeq; XP_008673571.1; XM_008675349.1.
DR AlphaFoldDB; B4FWI4; -.
DR EnsemblPlants; Zm00001eb040890_T001; Zm00001eb040890_P001; Zm00001eb040890.
DR Gramene; Zm00001eb040890_T001; Zm00001eb040890_P001; Zm00001eb040890.
DR HOGENOM; CLU_019796_8_1_1; -.
DR InParanoid; B4FWI4; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; B4FWI4; baseline and differential.
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; 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; IPR015878; Ado_hCys_hydrolase_NAD-bd.
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:SF20; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 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 SMART; SM00997; AdoHcyase_NAD; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B4FWI4};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 552..624
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 624 AA; 65285 MW; 76F00760FE1DEB97 CRC64;
MAASRALLPS PQVSPASARV RLAAAVPSSL TLAARGGAGA GARLRVRCAI LSSPAPVAPT
ESRPVRRISP SAPDGALRPK PAVLVAEKLS EAGLAVLRQF ADVECAYGMS PAELLAKAAQ
FDALIVRSGT KVTREVLEAG QGRLRVVGRA GVGIDNVDLQ AATEVGCLVV NAPTANTIAA
AEHGIALLAS MARNVSQADA ALKAGKWQRN KYVGVSLVGK TLAVMGFGKV GSEVARRAKG
LGMHVIAHDP YAPADRARAL GVELVSFDEA IARADFISLH MPLIPTTSKI FNDESFAKMK
TGVRIINVAR GGVIDEDALV RALDSGKVAQ AALDVFTVEP PPKDSKLVLH ENVTVTPHLG
ASTVEAQEGV AIEIAEAVVG ALRGELAATA VNAPMVPAEI LSELAPYVSL AEKLGRLAVQ
LVAGESGIKG VKVVYTTARG PDDLDTRLLR AMVTKGLVEP VSSTFVNLVN ADYTAKQRGL
RLTEERVAHD SPAAEAPLES VQVRLSHVQS KFAGAISDGG DDIVLEGRVK YGVPHLTLVG
PYEVDVSLEG NLILCRQIDQ PGMIGKVGNI LGDTNVNINF MSVGRTFRGK QAIMAIGVDE
EPDKDTLEKI GAIPAIEEFV FLEL
//
