ID A0A0D2VZL5_GOSRA Unreviewed; 600 AA.
AC A0A0D2VZL5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN ORFNames=B456_012G149100 {ECO:0000313|EMBL:KJB77655.1}, Gorai_004842
GN {ECO:0000313|EMBL:MBA0601671.1};
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:KJB77655.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB77655.1, 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).
RN [2] {ECO:0000313|EMBL:MBA0601671.1, ECO:0000313|Proteomes:UP000593578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:MBA0601671.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0601671.1};
RX PubMed=30476109;
RA Grover C.E., Arick M.A. 2nd, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Frelichowski J.E., Scheffler J.A., Scheffler B.E.,
RA Wendel J.F.;
RT "Insights into the Evolution of the New World Diploid Cottons (Gossypium,
RT Subgenus Houzingenia) Based on Genome Sequencing.";
RL Genome Biol. Evol. 11:53-71(2019).
RN [3] {ECO:0000313|EMBL:MBA0601671.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8 {ECO:0000313|EMBL:MBA0601671.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0601671.1};
RA Grover C.E., Arick M.A. II, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Scheffler J.A., Scheffler B.E., Wendel J.F.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM001751; KJB77655.1; -; Genomic_DNA.
DR EMBL; JABEZZ010000012; MBA0601671.1; -; Genomic_DNA.
DR RefSeq; XP_012459242.1; XM_012603788.1.
DR AlphaFoldDB; A0A0D2VZL5; -.
DR STRING; 29730.A0A0D2VZL5; -.
DR EnsemblPlants; KJB77655; KJB77655; B456_012G149100.
DR GeneID; 105779839; -.
DR Gramene; KJB77655; KJB77655; B456_012G149100.
DR KEGG; gra:105779839; -.
DR eggNOG; KOG0068; Eukaryota.
DR OMA; MLNNETF; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000032304; Chromosome 12.
DR Proteomes; UP000593578; Unassembled 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; 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:SF22; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 528..600
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 600 AA; 63557 MW; 02CB4403477CCF4A CRC64;
MASLKIPTLK TPSHSLSSKL SLRSAFSANF PNSAHFSRSQ PQRGRVLIIT SAASSSSSNK
PTVLVAEKLG EAGLTLLKEF ADVDCSYNLS PEELRSKISL CDALIVRSGT KVNRAVFESS
GGRLKVVGRA GVGIDNVDLA AATEHGCLVV NAPTANTVAA AEHGIALLAA MARNVAQADA
SIKSGKWQRN KYVGVSLVGK TLAVLGFGKV GSEVARRAKG LGMHVIAHDP YAPAERARAI
GVELVSFDEA IGAADFISMH MPLTPATSNM LNNETFAKMK KGVRIVNVAR GGVVDEEALV
RALDAGIVAQ AALDVFSEEP PKQDNKLVQH EMVTVTPHLG ASTMEAQEGV AIEIAEAVVG
ALKGELAATA VNAPMVPAEV LLELKPYVIL AEKLGRLAVQ LVAGGSGVKT VKVSYASSRP
DLDTRLLRAM ITKGIIEPIS DIYVNLVNAD YTAKQRGLRI TEEHIHLDGS HEIPLEFIKV
QIANVKSKFA SATSKSGEIK VEGRVKDGIP HLTKVGSFRV DVSLEGSIIL CRQVDQPGMI
GKVGSILGEE NVNVSFMSVG RVAPRKHAVM AIGVDDQPRK ESLKRIGEVP AIEESVFLKL
//
