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Protein

Serine hydroxymethyltransferase

Gene

glyA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=7 µM for tetrahydrofolate2 Publications
  2. KM=140 µM for serine2 Publications
  3. KM=300 µM for serine2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tetrahydrofolate interconversion

    This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
    View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

    Pathwayi: glycine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes glycine from L-serine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Serine hydroxymethyltransferase (glyA)
    This subpathway is part of the pathway glycine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from L-serine, the pathway glycine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei35Pyridoxal phosphate2 Publications1
    Binding sitei55Pyridoxal phosphate2 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei55Transaldimination and stability1
    Binding sitei57Substrate1
    Binding sitei64Substrate1
    Binding sitei65Pyridoxal phosphate2 Publications1
    Binding sitei99Pyridoxal phosphate2 Publications1
    Binding sitei121Substrate; via carbonyl oxygen1
    Binding sitei175Pyridoxal phosphate2 Publications1
    Binding sitei203Pyridoxal phosphate2 Publications1
    Binding sitei228Pyridoxal phosphate2 Publications1
    Binding sitei235Pyridoxal phosphate2 Publications1
    Sitei235Transaldimination and stability1
    Binding sitei246Substrate1
    Binding sitei263Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen2 Publications1
    Binding sitei363Pyridoxal phosphate2 Publications1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • amino acid binding Source: GO_Central
    • cobalt ion binding Source: GO_Central
    • glycine hydroxymethyltransferase activity Source: EcoCyc
    • identical protein binding Source: IntAct
    • pyridoxal phosphate binding Source: EcoCyc
    • serine binding Source: GO_Central
    • zinc ion binding Source: EcoliWiki

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionTransferase
    Biological processAmino-acid biosynthesis, One-carbon metabolism
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:GLYOHMETRANS-MONOMER
    MetaCyc:GLYOHMETRANS-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.2.1 2026
    4.1.2.48 2026

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00193

    UPA00288;UER01023

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Serine hydroxymethyltransferase (EC:2.1.2.1)
    Short name:
    SHMT
    Short name:
    Serine methylase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:glyA
    Ordered Locus Names:b2551, JW2535
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...
    EcoGenei
    EG10408 glyA

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi55Y → F: 50 and 15-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 4-fold decrease in the catalytic efficiency. 1 Publication1
    Mutagenesisi65Y → F: Decrease in catalytic activity. 1 Publication1
    Mutagenesisi85L → A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-276. 1 Publication1
    Mutagenesisi214P → A: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication1
    Mutagenesisi214P → G: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication1
    Mutagenesisi216P → A: No significant difference in catalytic efficiency and affinity compared to the wild-type. Alteration in the folding rate. 1 Publication1
    Mutagenesisi216P → G: Important decrease in affinity and catalytic efficiency. Severely compromised in folding into a catalytically competent enzyme. 1 Publication1
    Mutagenesisi218P → A: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication1
    Mutagenesisi218P → G: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication1
    Mutagenesisi235R → K: 1500- and 20-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 15-fold decrease in the catalytic efficiency. 1 Publication1
    Mutagenesisi235R → L: 450- and 11-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 60-fold decrease in the catalytic efficiency. 1 Publication1
    Mutagenesisi235R → Q: 900- and 17-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 30-fold decrease in the catalytic efficiency. 1 Publication1
    Mutagenesisi258P → A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability. 1 Publication1
    Mutagenesisi258P → G: Important decrease in affinity and catalytic efficiency. 1 Publication1
    Mutagenesisi264P → A: Important decrease in affinity and catalytic efficiency. 1 Publication1
    Mutagenesisi264P → G: Important decrease in affinity and catalytic efficiency. 1 Publication1
    Mutagenesisi276L → A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-85. 1 Publication1
    Mutagenesisi363R → A: It does not bind serine and glycine and shows no activity with serine as the substrate. 1 Publication1
    Mutagenesisi363R → K: Exhibits only 0.03% of the catalytic activity of the wild-type and a 15-fold reduction in affinity for glycine and serine. 1 Publication1
    Mutagenesisi372R → A: No significant difference compared to the wild-type. 1 Publication1
    Mutagenesisi372R → K: No significant difference compared to the wild-type. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001135731 – 417Serine hydroxymethyltransferaseAdd BLAST417

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei54N6-acetyllysine1 Publication1
    Modified residuei62N6-succinyllysine1 Publication1
    Modified residuei229N6-(pyridoxal phosphate)lysine1
    Modified residuei242N6-succinyllysine1 Publication1
    Modified residuei250N6-acetyllysine; alternate1 Publication1
    Modified residuei250N6-succinyllysine; alternate1 Publication1
    Modified residuei277N6-succinyllysine1 Publication1
    Modified residuei285N6-acetyllysine1 Publication1
    Modified residuei293N6-succinyllysine1 Publication1
    Modified residuei331N6-succinyllysine1 Publication1
    Modified residuei346N6-succinyllysine1 Publication1
    Modified residuei354N6-acetyllysine; alternate1 Publication1
    Modified residuei354N6-succinyllysine; alternate1 Publication1
    Modified residuei375N6-acetyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0A825

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P0A825

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0A825

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...
    SWISS-2DPAGEi
    P0A825

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P0A825

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    By CsgD.1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-909080,EBI-909080

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4261314, 221 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-36205N

    Protein interaction database and analysis system

    More...
    IntActi
    P0A825, 8 interactors

    Molecular INTeraction database

    More...
    MINTi
    P0A825

    STRING: functional protein association networks

    More...
    STRINGi
    316385.ECDH10B_2718

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1417
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P0A825

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P0A825

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P0A825

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni125 – 127Substrate binding3
    Regioni355 – 357Substrate binding3

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the SHMT family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105C65 Bacteria
    COG0112 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000239404

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0A825

    KEGG Orthology (KO)

    More...
    KOi
    K00600

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0A825

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00378 SHMT, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.640.10, 1 hit
    3.90.1150.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00051 SHMT, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR015424 PyrdxlP-dep_Trfase
    IPR015422 PyrdxlP-dep_Trfase_dom1
    IPR015421 PyrdxlP-dep_Trfase_major
    IPR001085 Ser_HO-MeTrfase
    IPR019798 Ser_HO-MeTrfase_PLP_BS
    IPR039429 SHMT-like_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11680 PTHR11680, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00464 SHMT, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000412 SHMT, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53383 SSF53383, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00096 SHMT, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P0A825-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ
    60 70 80 90 100
    LTNKYAEGYP GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ
    110 120 130 140 150
    ANFAVYTALL EPGDTVLGMN LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT
    160 170 180 190 200
    GHIDYADLEK QAKEHKPKMI IGGFSAYSGV VDWAKMREIA DSIGAYLFVD
    210 220 230 240 250
    MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL AKGGSEELYK
    260 270 280 290 300
    KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE
    310 320 330 340 350
    VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP
    360 370 380 390 400
    NDPKSPFVTS GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE
    410
    RIKGKVLDIC ARYPVYA
    Length:417
    Mass (Da):45,317
    Last modified:July 21, 1986 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i13E5558E99938539
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    V00283 Genomic DNA Translation: CAA23547.1
    U00096 Genomic DNA Translation: AAC75604.1
    AP009048 Genomic DNA Translation: BAA16459.1
    J01620 Genomic DNA Translation: AAA23912.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A00559 XYECS

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417046.1, NC_000913.3
    WP_000919159.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75604; AAC75604; b2551
    BAA16459; BAA16459; BAA16459

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947022

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2535
    eco:b2551

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4183

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00283 Genomic DNA Translation: CAA23547.1
    U00096 Genomic DNA Translation: AAC75604.1
    AP009048 Genomic DNA Translation: BAA16459.1
    J01620 Genomic DNA Translation: AAA23912.1
    PIRiA00559 XYECS
    RefSeqiNP_417046.1, NC_000913.3
    WP_000919159.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1DFOX-ray2.40A/B/C/D1-417[»]
    1EQBX-ray2.70A/B/C/D1-417[»]
    3G8MX-ray3.30A1-417[»]
    ProteinModelPortaliP0A825
    SMRiP0A825
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261314, 221 interactors
    DIPiDIP-36205N
    IntActiP0A825, 8 interactors
    MINTiP0A825
    STRINGi316385.ECDH10B_2718

    PTM databases

    iPTMnetiP0A825

    2D gel databases

    SWISS-2DPAGEiP0A825

    Proteomic databases

    EPDiP0A825
    PaxDbiP0A825
    PRIDEiP0A825

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75604; AAC75604; b2551
    BAA16459; BAA16459; BAA16459
    GeneIDi947022
    KEGGiecj:JW2535
    eco:b2551
    PATRICifig|1411691.4.peg.4183

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB0403
    EcoGeneiEG10408 glyA

    Phylogenomic databases

    eggNOGiENOG4105C65 Bacteria
    COG0112 LUCA
    HOGENOMiHOG000239404
    InParanoidiP0A825
    KOiK00600
    PhylomeDBiP0A825

    Enzyme and pathway databases

    UniPathwayi
    UPA00193

    UPA00288;UER01023

    BioCyciEcoCyc:GLYOHMETRANS-MONOMER
    MetaCyc:GLYOHMETRANS-MONOMER
    BRENDAi2.1.2.1 2026
    4.1.2.48 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A825

    Protein Ontology

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    PROi
    PR:P0A825

    Family and domain databases

    CDDicd00378 SHMT, 1 hit
    Gene3Di3.40.640.10, 1 hit
    3.90.1150.10, 1 hit
    HAMAPiMF_00051 SHMT, 1 hit
    InterProiView protein in InterPro
    IPR015424 PyrdxlP-dep_Trfase
    IPR015422 PyrdxlP-dep_Trfase_dom1
    IPR015421 PyrdxlP-dep_Trfase_major
    IPR001085 Ser_HO-MeTrfase
    IPR019798 Ser_HO-MeTrfase_PLP_BS
    IPR039429 SHMT-like_dom
    PANTHERiPTHR11680 PTHR11680, 1 hit
    PfamiView protein in Pfam
    PF00464 SHMT, 1 hit
    PIRSFiPIRSF000412 SHMT, 1 hit
    SUPFAMiSSF53383 SSF53383, 1 hit
    PROSITEiView protein in PROSITE
    PS00096 SHMT, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLYA_ECOLI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A825
    Secondary accession number(s): P00477
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: December 5, 2018
    This is version 116 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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