ID V4KYF7_EUTSA Unreviewed; 625 AA.
AC V4KYF7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN ORFNames=EUTSA_v10007072mg {ECO:0000313|EMBL:ESQ35022.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ35022.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ35022.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(2013).
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; KI517683; ESQ35022.1; -; Genomic_DNA.
DR RefSeq; XP_006416669.1; XM_006416606.1.
DR AlphaFoldDB; V4KYF7; -.
DR STRING; 72664.V4KYF7; -.
DR EnsemblPlants; ESQ35022; ESQ35022; EUTSA_v10007072mg.
DR GeneID; 18993124; -.
DR Gramene; ESQ35022; ESQ35022; EUTSA_v10007072mg.
DR KEGG; eus:EUTSA_v10007072mg; -.
DR eggNOG; KOG0068; Eukaryota.
DR OMA; NLECAYN; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000030689; 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; 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; 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|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:UP000030689};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 86..395
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 188..363
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 407..520
FT /note="D-3-phosphoglycerate dehydrogenase ASB"
FT /evidence="ECO:0000259|Pfam:PF19304"
FT DOMAIN 554..611
FT /note="ACT"
FT /evidence="ECO:0000259|Pfam:PF01842"
SQ SEQUENCE 625 AA; 66617 MW; 29CAA6A5217F3F4D CRC64;
MAISSSCSTV KAVNTRWTSP SLSPVSKFAV LRRLSLLPEL RYTQNVKLTA TNALRTFEQT
TLTEDHKFST VGSDEDDSAS FPKPRILVAE KLGEAGVNLL RGFGDVDCSY ELSPEDLKKK
VAESDALIVR SGTKVTREVF EAAKGRLKVV GRAGVGIDNV DLQAATEYGC LVVNAPTANT
VAAAEHGIAL LASMARNVAQ ADASIKAGKW ERSKYVGVSL VGKTLAVMGF GKVGTEVARR
AKGLGMNVIS HDPYAPADRA RALGVDLVSF DQAIATADFV SLHMPLTPAT KKVFNDQTFS
KMKKGVRLIN VARGGVIDED ALVRALDSGI VAQAALDVFC EEPPSKDSKL IQHENVTVTP
HLGASTKEAQ EGVAIEIAEA VAGALKGELS ATAVNAPMVA PEVLSELAPY IVLAEKLGRL
AVQLASGGKG VQSIKVVYRS ARDRDDLDTR LLRAMITKGI IEPISDSYVN LVNADFIAKQ
KGLRISEERM VVDSSPEYPV DSIQVQISNV ESSFAGAVSD CGAISIEGRV KYGVPHLTCV
GSFAVDVSLE GNLILCRQVD QPGMIGQVGN ILGEQNVNVN FMSVGRRVVR KQAIMAIGVD
EEPDNKTLER IGGVSAIEEF VFLKL
//
