GenomeNet

Database: UniProt
Entry: Q9LT69
LinkDB: Q9LT69
Original site: Q9LT69 
ID   SERA3_ARATH             Reviewed;         588 AA.
AC   Q9LT69; Q94B47;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   13-FEB-2019, entry version 134.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase 3, chloroplastic;
DE            EC=1.1.1.95 {ECO:0000269|PubMed:24368794};
DE   Flags: Precursor;
GN   Name=PGDH3; Synonyms=3-PGDH; OrderedLocusNames=At3g19480;
GN   ORFNames=MLD14.22;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-588.
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=24368794; DOI=10.1105/tpc.113.118992;
RA   Benstein R.M., Ludewig K., Wulfert S., Wittek S., Gigolashvili T.,
RA   Frerigmann H., Gierth M., Fluegge U.I., Krueger S.;
RT   "Arabidopsis phosphoglycerate dehydrogenase1 of the phosphoserine
RT   pathway is essential for development and required for ammonium
RT   assimilation and tryptophan biosynthesis.";
RL   Plant Cell 25:5011-5029(2013).
RN   [5]
RP   FUNCTION, GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24058165; DOI=10.1104/pp.113.226720;
RA   Toujani W., Munoz-Bertomeu J., Flores-Tornero M., Rosa-Tellez S.,
RA   Anoman A.D., Alseekh S., Fernie A.R., Ros R.;
RT   "Functional characterization of the plastidial 3-phosphoglycerate
RT   dehydrogenase family in Arabidopsis.";
RL   Plant Physiol. 163:1164-1178(2013).
CC   -!- FUNCTION: Involved in the plastidial phosphorylated pathway of
CC       serine biosynthesis (PPSB). {ECO:0000269|PubMed:24058165,
CC       ECO:0000269|PubMed:24368794}.
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:0000269|PubMed:24368794};
CC   -!- ACTIVITY REGULATION: Partially inhibited by 1 mM serine.
CC       {ECO:0000269|PubMed:24368794}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.006 mM for 3-phospho-D-glycerate (at pH 8.1)
CC         {ECO:0000269|PubMed:24368794};
CC         KM=0.239 mM for NAD(+) (at pH 8.1)
CC         {ECO:0000269|PubMed:24368794};
CC         KM=2.559 mM for 3-phospho-D-glycerate (at pH 7.2)
CC         {ECO:0000269|PubMed:24368794};
CC         KM=0.551 mM for NAD(+) (at pH 7.2)
CC         {ECO:0000269|PubMed:24368794};
CC         Vmax=137.6 umol/min/mg enzyme (at pH 8.1)
CC         {ECO:0000269|PubMed:24368794};
CC         Vmax=93.7 umol/min/mg enzyme (at pH 7.2)
CC         {ECO:0000269|PubMed:24368794};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
CC   -!- TISSUE SPECIFICITY: Expressed in aerial parts. Not detected in
CC       roots and meristematic tissue. Expressed in cotyledons, adult
CC       leaves, stigma and anther filaments. Detected in the embryo.
CC       {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
CC   -!- INDUCTION: Up-regulated in the aerial parts by dark treatment. Not
CC       regulated by high CO(2) levels. {ECO:0000269|PubMed:24058165}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:24058165}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AB025624; BAB02473.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76246.1; -; Genomic_DNA.
DR   EMBL; AY042858; AAK68798.1; -; mRNA.
DR   RefSeq; NP_566637.2; NM_112835.4.
DR   UniGene; At.46279; -.
DR   UniGene; At.68436; -.
DR   ProteinModelPortal; Q9LT69; -.
DR   SMR; Q9LT69; -.
DR   STRING; 3702.AT3G19480.1; -.
DR   iPTMnet; Q9LT69; -.
DR   PaxDb; Q9LT69; -.
DR   PRIDE; Q9LT69; -.
DR   ProMEX; Q9LT69; -.
DR   EnsemblPlants; AT3G19480.1; AT3G19480.1; AT3G19480.
DR   GeneID; 821482; -.
DR   Gramene; AT3G19480.1; AT3G19480.1; AT3G19480.
DR   KEGG; ath:AT3G19480; -.
DR   Araport; AT3G19480; -.
DR   TAIR; locus:2090649; AT3G19480.
DR   eggNOG; KOG0068; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136693; -.
DR   InParanoid; Q9LT69; -.
DR   KO; K00058; -.
DR   OMA; MLNNETF; -.
DR   OrthoDB; 911009at2759; -.
DR   PhylomeDB; Q9LT69; -.
DR   BioCyc; ARA:AT3G19480-MONOMER; -.
DR   Reactome; R-ATH-977347; Serine biosynthesis.
DR   UniPathway; UPA00135; UER00196.
DR   PRO; PR:Q9LT69; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   Genevisible; Q9LT69; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1330.90; -; 1.
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   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   SMART; SM00997; AdoHcyase_NAD; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 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   Chloroplast; Complete proteome; NAD; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     38       Chloroplast. {ECO:0000255}.
FT   CHAIN        39    588       D-3-phosphoglycerate dehydrogenase 3,
FT                                chloroplastic.
FT                                /FTId=PRO_0000430237.
FT   DOMAIN      516    588       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
FT   NP_BIND     195    196       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     274    276       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   NP_BIND     324    327       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   ACT_SITE    276    276       {ECO:0000250}.
FT   ACT_SITE    305    305       {ECO:0000250}.
FT   ACT_SITE    324    324       Proton donor. {ECO:0000250}.
FT   BINDING     215    215       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
FT   BINDING     300    300       NAD. {ECO:0000250|UniProtKB:P0A9T0}.
SQ   SEQUENCE   588 AA;  62122 MW;  E4C9A35BE86D3AD5 CRC64;
     MATSLNLSSI FSSSSRLVTT PSSVFPIRQR RRIILVTSSS SGGGGKPTIL VTEKLGQAGI
     DLLKKYANVD CSYDLSLEEL CTKISLCDAL IVRSGTKVGR DVFESSRGRL KVVGRAGVGI
     DNVDLAAATE YGCLVVNAPT ANTVAAAEHG IALLTAMARN IAQADASIKA GKWTRNKYVG
     VSLVGKTLAV LGFGKVGSEV ARRARGLGMH VITHDPYAPA DRARAIGVEL VSFEVAISTA
     DFISLHLPLT AATSKMMNDV TFAMMKKGVR IVNVARGGVI DEEALLRALD SGIVAQAALD
     VFTVEPPVKD NKLVLHESVT ATPHLGASTM EAQEGVSIEV AEAVIGALRG ELAATAVNAP
     MVPLEVLREL KPYVVLAEKL GRLAVQLVTG GSGVNAVKVT YASSRAPDDL DTRLLRAMVI
     KGIIEPISSV FINLVNSDYI AKQRGVKISE ERMVLDGSPE NPIEYITVRI ANVESRFASA
     LSESGEIKVE GRVKQGVPSL TKVGLFGVDV SLEGSVILCR QVDQPGMIGK VASILGDENV
     NVSFMSVGRI APGKQAVMAI GVDEQPSKET LKKIGDIPAI EEFVFLKL
//
DBGET integrated database retrieval system