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Database: UniProt
Entry: A0A0D2V4E2_GOSRA
LinkDB: A0A0D2V4E2_GOSRA
Original site: A0A0D2V4E2_GOSRA 
ID   A0A0D2V4E2_GOSRA        Unreviewed;       560 AA.
AC   A0A0D2V4E2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00013143};
DE            EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
GN   ORFNames=B456_010G023200 {ECO:0000313|EMBL:KJB63880.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB63880.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB63880.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
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   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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DR   EMBL; CM001749; KJB63880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2V4E2; -.
DR   EnsemblPlants; KJB63880; KJB63880; B456_010G023200.
DR   Gramene; KJB63880; KJB63880; B456_010G023200.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000032304; Chromosome 10.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR045626; PGDH_ASB_dom.
DR   PANTHER; PTHR42938:SF6; 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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT   DOMAIN          488..560
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   560 AA;  59677 MW;  E2E403A0FC47128E CRC64;
     MSVISSWNLT ISLNTTLSLS WRSSLPSRAI FPRPKKSKTL VVLAIALGAK PTVLVSEKLG
     DAGIQLLKTF ANVDCSYNLS PEELCTKISL CDALIVRSGT KVTREVFESA MGRLKVVGRA
     GVGIDNVDIS AATEHGCLVV NAPTANTIAA AEHGIALLTA VSRNVAQADA SVKAGKWERN
     KYVGVSLVGK TLAVMGFGKV GSEVARRAKG LGMQVIAHDP YAPADRARAI GVELVSFEEA
     LTTADFISLH MPLTPATSKM FNDEAFSRVK KGVRIINVAR GGVIDEEALL RALDSGIVAQ
     AALDVFTEEP PPQENKLVRH ENVTVTPHLG ASTTEAQVLL ELSPYVALTE KLGRLAVQLV
     AGGSGVKFVK VTYASARGPD DLDTRLLRAM VTKGLIEPIS SVFVNLVNAD FIGKQRGLRL
     TEERIVLDGS PEKPLEFIQV RIANVESKFA SAISNSGEIT VEGRVKDGKP HLTKVGSFGV
     DVSLEGSIVL CRQSDQPGII GKVGNILSEE NVNVNFMSVG RIAPGKQAVM TIGLDEEPSR
     DALKKIGEIT AVEEFVFLKL
//
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