serA [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

Go to the top of the page Help

Official Symbol: serA
Primary source: ECOCYC:EG10944
Locus tag: b2913
See related: ASAP:ABE-0009561
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK2909
Summary: D-3-phosphoglycerate dehydrogenase catalyzes the first committed step in the biosynthesis of L-serine. [More information is available at EcoCyc: EG10944].
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Sequence:: NC_000913.3 (3057178..3058410, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Inhibition of glycine cleavage system by pyridoxine 5'-phosphate causes synthetic lethality in glyA yggS and serA yggS in Escherichia coli.
Title: Inhibition of glycine cleavage system by pyridoxine 5'-phosphate causes synthetic lethality in glyA yggS and serA yggS in Escherichia coli.
Data indicate that the cooperative transmission induced by serine binding is transmitted through the D-3-phosphoglycerate dehydrogenase Gly294-Gly295 hinge region to the opposite serine binding interface.
Title: Transient kinetic analysis of L-serine interaction with Escherichia coli D-3-phosphoglycerate dehydrogenase containing amino acid mutations in the hinge regions.
L-serine, inhibitor of D-3-phosphoglycerate dehydrogenase, exerts its effect on at least two steps in the kinetic mechanism, but to very different degrees.
Title: Transient kinetic analysis of the interaction of L-serine with Escherichia coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector binding.
the rate-limiting step in both directions is a conformational change in the Escherichia coli D-3-phosphoglycerate dehydrogenase enzyme that is not detected optically
Title: A stopped flow transient kinetic analysis of substrate binding and catalysis in Escherichia coli D-3-phosphoglycerate dehydrogenase.
N-terminus verified by Edman degradation on mature peptide
Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
crystal structure
Title: Vmax regulation through domain and subunit changes. The active form of phosphoglycerate dehydrogenase.
analysis of mutation effects on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase
Title: The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase.
L-Serine inhibits the catalytic activity of D-3-phosphoglycerate dehydrogenase by binding to its regulatory domain.
Title: Identification of amino acid residues contributing to the mechanism of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.

Submit: New GeneRIF Correction

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables 2-hydroxyglutarate dehydrogenase activity	IDA Inferred from Direct Assay more info	PubMed
enables NAD binding	IEA Inferred from Electronic Annotation more info
enables NAD+ binding	IDA Inferred from Direct Assay more info	PubMed
enables NADH binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor	IEA Inferred from Electronic Annotation more info
enables phosphoglycerate dehydrogenase activity	IDA Inferred from Direct Assay more info	PubMed
enables phosphoglycerate dehydrogenase activity	IEA Inferred from Electronic Annotation more info
enables serine binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in L-serine biosynthetic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within L-serine biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: phosphoglycerate dehydrogenase

NP_417388.1

EC 1.1.1.399

EC 1.1.1.95

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

3057178..3058410 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417388.1 phosphoglycerate dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_417388.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0AAI9PXT0

Conserved Domains (1) summary

PRK11790
Location:1 → 410

PRK11790; phosphoglycerate dehydrogenase