T00247
type: Enzyme
cath: Rossmann fold
cath: Alpha-Beta Plaits
ec: https://purl.uniprot.org/enzyme/1.1.1.95
csa: 1psd
uniprot: P0A9T0
kegg enzyme: phosphoglycerate dehydrogenase
kegg enzyme: D-3-phosphoglycerate:NAD+ oxidoreductase
kegg enzyme: alpha-phosphoglycerate dehydrogenase
kegg enzyme: 3-phosphoglycerate dehydrogenase
kegg enzyme: 3-phosphoglyceric acid dehydrogenase
kegg enzyme: D-3-phosphoglycerate dehydrogenase
kegg enzyme: glycerate 3-phosphate dehydrogenase
kegg enzyme: glycerate-1,3-phosphate dehydrogenase
kegg enzyme: phosphoglycerate oxidoreductase
kegg enzyme: phosphoglyceric acid dehydrogenase
kegg enzyme: SerA
kegg enzyme: 3-phosphoglycerate:NAD+ 2-oxidoreductase
kegg enzyme: SerA 3PG dehydrogenase
kegg enzyme: 3PHP reductase
kegg enzyme: alphaKG reductase
kegg enzyme: D- and L-HGA
kegg pathway: Glycine, serine and threonine metabolism
kegg substrate: 3-Phosphoglycerate
kegg substrate: NAD+
kegg product: 3-Phosphohydroxypyruvate
kegg product: NADH
kegg product: H+
pdb: 1psdA01
pdb: 1psdB01
pdb: 1sc6A01
pdb: 1sc6B01
pdb: 1sc6C01
pdb: 1sc6D01
pdb: 1psdA02
pdb: 1psdB02
pdb: 1sc6A02
pdb: 1sc6B02
pdb: 1sc6C02
pdb: 1sc6D02
pdb: 1psdA03
pdb: 1psdB03
pdb: 1sc6A03
pdb: 1sc6B03
pdb: 1sc6C03
pdb: 1sc6D03
pdb bound state: Unbound
  compound: 3-Phosphoglycerate
  pdb: 1psdA01
pdb bound state: Unbound
  compound: 3-Phosphoglycerate
  pdb: 1psdB01
pdb bound state: Unbound
  compound: 3-Phosphoglycerate
  pdb: 1sc6A01
pdb bound state: Unbound
  compound: 3-Phosphoglycerate
  pdb: 1sc6B01
pdb bound state: Unbound
  compound: 3-Phosphoglycerate
  pdb: 1sc6C01
pdb bound state: Unbound
  compound: 3-Phosphoglycerate
  pdb: 1sc6D01
active site residues resources: P0A9T0
references: D-3-phosphoglycerate dehydrogenase from Escherichia coli: isolation by affinity chromatography and sequence comparison to other dehydrogenases.
references: Purification and subunit structure of phosphoglycerate dehydrogenase from rabbit liver.
references: The nucleotide sequence of the serA gene of Escherichia coli and the amino acid sequence of the encoded protein, D-3-phosphoglycerate dehydrogenase.
references: A new family of 2-hydroxyacid dehydrogenases.
references: Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12.
references: Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.
references: The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase.
references: The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding.
references: The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Site-directed mutagenesis of effector binding site residues.
references: A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme.
references: Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase.
references: Probing the regulatory domain interface of D-3-phosphoglycerate dehydrogenase with engineered tryptophan residues.
references: Phosphate ion partially relieves the cooperativity of effector binding in D-3-phosphoglycerate dehydrogenase without altering the cooperativity of inhibition.
references: The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase.
references: The relationship between effector binding and inhibition of activity in D-3-phosphoglycerate dehydrogenase.
references: Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects.
references: Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase.
references: Molecular cloning, sequence and characterization of a novel streptococcal phosphoglycerate dehydrogenase gene.
references: Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase.
references: Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase.
references: 3-Phosphoglycerate dehydrogenase from Corynebacterium glutamicum: the C-terminal domain is not essential for activity but is required for inhibition by L-serine.
references: De-regulation of D-3-phosphoglycerate dehydrogenase by domain removal. Eur J Biochem. 2002 Sep;269(17):4176-84.
references: Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.
references: Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
references: Multiconformational states in phosphoglycerate dehydrogenase.
references: Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.5600

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720
catalytic domain: index.html

Alpha-Beta Plaits
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.70.260

Glycine, serine and threonine metabolism
type: KeggPathway
references: KEGG:MAP00260

3-Phosphoglycerate
type: KeggSubstrate
references: KEGG:C00597
compound type: carbohydrate
compound type: carboxyl group
compound type: phosphate group/phosphate ion
references: CHEBI:17050
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NAD+
type: KeggSubstrate
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

3-Phosphohydroxypyruvate
type: KeggProduct
references: KEGG:C03232
compound type: carbohydrate
compound type: carboxyl group
compound type: phosphate group/phosphate ion
references: CHEBI:30933
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggProduct
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1psdA02
type: Pdb
references: 1psd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psd
catalytic residue: ARG 240;GLU 269;HIS 292

1psdB02
type: Pdb
references: 1psd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1psd
catalytic residue: ARG 240;GLU 269;HIS 292

1sc6A02
type: Pdb
references: 1sc6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sc6
catalytic residue: ARG 240; ;HIS 292
comment: invisible 266-274, mutant W139G

1sc6B02
type: Pdb
references: 1sc6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sc6
catalytic residue: ARG 240; ;HIS 292
comment: invisible 266-274, mutant W139G

1sc6C02
type: Pdb
references: 1sc6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sc6
catalytic residue: ARG 240; ;
comment: invisible 266-274/292-298 mutant W139G

1sc6D02
type: Pdb
references: 1sc6
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1sc6
catalytic residue: ARG 240; ;
comment: invisible 266-274/292-295 mutant W139G

D-3-phosphoglycerate dehydrogenase from Escherichia coli: isolation by affinity chromatography and sequence comparison to other dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7049261
journal: Biosci Rep
volume: 1
pages: 733-41
published year: 1981
authors:
  item: vGrant GA
  item: Zapp ML

Purification and subunit structure of phosphoglycerate dehydrogenase from rabbit liver.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3800969
journal: Biochem J
volume: 238
pages: 919-22
published year: 1986
authors:
  item: Lund K
  item: Merrill DK
  item: Guynn RW

The nucleotide sequence of the serA gene of Escherichia coli and the amino acid sequence of the encoded protein, D-3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/3017965
journal: J Biol Chem
volume: 261
pages: 12179-83
published year: 1986
authors:
  item: Tobey KL
  item: Grant GA

A new family of 2-hydroxyacid dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2692566
journal: Biochem Biophys Res Commun
volume: 165
pages: 1371-4
published year: 1989
authors:
  item: Grant GA

Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/2681152
journal: J Bacteriol
volume: 171
pages: 6084-92
published year: 1989
authors:
  item: Schoenlein PV
  item: Roa BB
  item: Winkler ME

Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1567457
journal: Biochem Biophys Res Commun
volume: 184
pages: 60-6
published year: 1992
authors:
  item: Kochhar S
  item: Hunziker PE
  item: Leong-Morgenthaler P
  item: Hottinger H

The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
references: http://www.ncbi.nlm.nih.gov/pubmed/7719856
journal: Nat Struct Biol
volume: 2
pages: 69-76
published year: 1995
authors:
  item: Schuller DJ
  item: Grant GA
  item: Banaszak LJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0A9T0

The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8662776
journal: J Biol Chem
volume: 271
pages: 13013-7
published year: 1996
authors:
  item: Al-Rabiee R
  item: Lee EJ
  item: Grant GA

The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Site-directed mutagenesis of effector binding site residues.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8798520
journal: J Biol Chem
volume: 271
pages: 23235-8
published year: 1996
authors:
  item: Al-Rabiee R
  item: Zhang Y
  item: Grant GA

A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8771194
journal: Protein Sci
volume: 5
pages: 34-41
published year: 1996
authors:
  item: Grant GA
  item: Schuller DJ
  item: Banaszak LJ

Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9163325
journal: Biochem J
volume: 323
pages: 365-70
published year: 1997
authors:
  item: Achouri Y
  item: Rider MH
  item: Schaftingen EV
  item: Robbi M

Probing the regulatory domain interface of D-3-phosphoglycerate dehydrogenase with engineered tryptophan residues.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9712860
journal: J Biol Chem
volume: 273
pages: 22389-94
published year: 1998
authors:
  item: Grant GA
  item: Xu XL

Phosphate ion partially relieves the cooperativity of effector binding in D-3-phosphoglycerate dehydrogenase without altering the cooperativity of inhibition.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10600116
journal: Biochemistry
volume: 38
pages: 16548-52
published year: 1999
authors:
  item: Grant GA
  item: Xu XL
  item: Hu Z
  item: Purvis AR

The contribution of adjacent subunits to the active sites of D-3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10026144
journal: J Biol Chem
volume: 274
pages: 5357-61
published year: 1999
authors:
  item: Grant GA
  item: Kim SJ
  item: Xu XL
  item: Hu Z

The relationship between effector binding and inhibition of activity in D-3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10595555
journal: Protein Sci
volume: 8
pages: 2501-5
published year: 1999
authors:
  item: Grant GA
  item: Xu XL
  item: Hu Z

Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10683264
journal: Arch Biochem Biophys
volume: 375
pages: 171-4
published year: 2000
authors:
  item: Grant GA
  item: Xu XL
  item: Hu Z

Role of an interdomain Gly-Gly sequence at the regulatory-substrate domain interface in the regulation of Escherichia coli. D-3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10852732
journal: Biochemistry
volume: 39
pages: 7316-9
published year: 2000
authors:
  item: Grant GA
  item: Xu XL
  item: Hu Z

Molecular cloning, sequence and characterization of a novel streptococcal phosphoglycerate dehydrogenase gene.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11155166
journal: Oral Microbiol Immunol
volume: 15
pages: 58-62
published year: 2000
authors:
  item: Kawabata S
  item: Terao Y
  item: Hamada S

Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11050089
journal: J Biol Chem
volume: 276
pages: 1078-83
published year: 2001
authors:
  item: Grant GA
  item: Hu Z
  item: Xu XL

Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11278587
journal: J Biol Chem
volume: 276
pages: 17844-50
published year: 2001
authors:
  item: Grant GA
  item: Hu Z
  item: Xu XL

3-Phosphoglycerate dehydrogenase from Corynebacterium glutamicum: the C-terminal domain is not essential for activity but is required for inhibition by L-serine.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12466884
journal: Appl Microbiol Biotechnol
volume: 60
pages: 437-41
published year: 2002
authors:
  item: Peters-Wendisch P
  item: Netzer R
  item: Eggeling L
  item: Sahm H

De-regulation of D-3-phosphoglycerate dehydrogenase by domain removal. Eur J Biochem. 2002 Sep;269(17):4176-84.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12199695
journal: Eur J Biochem
volume: 269
pages: 4176-84
published year: 2002
authors:
  item: Bell JK
  item: Pease PJ
  item: Bell JE
  item: Grant GA
  item: Banaszak LJ

Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12183470
journal: J Biol Chem
volume: 277
pages: 39548-53
published year: 2002
authors:
  item: Grant GA
  item: Hu Z
  item: Xu XL

Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12644455
journal: J Biol Chem
volume: 278
pages: 18170-6
published year: 2003
authors:
  item: Grant GA
  item: Hu Z
  item: Xu XL

Multiconformational states in phosphoglycerate dehydrogenase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15035616
journal: Biochemistry
volume: 43
pages: 3450-8
published year: 2004
authors:
  item: Bell JK
  item: Grant GA
  item: Banaszak LJ
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/14718528
journal: J Biol Chem
volume: 279
pages: 13452-60
published year: 2004
authors:
  item: Grant GA
  item: Xu XL
  item: Hu Z

ReferenceForCatalyticMechanism
reference index: 7
reference section: p.73

ReferenceForCatalyticMechanism
reference index: 25
reference section: p.3456-3458