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Entry version 192 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
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Protein

Formate-dependent phosphoribosylglycinamide formyltransferase

Gene

purT

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

Involved in the de novo purine biosynthesis (PubMed:8501063, PubMed:8117714, PubMed:9184151).

Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) (PubMed:8501063, PubMed:8117714, PubMed:9184151).

Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate (PubMed:8226647).

PurT is also able to cleave acetyl phosphate and carbamoyl phosphate to produce ATP with acetate and carbamate, respectively (PubMed:8117714, PubMed:9184151).

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 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

kcat is 37.6 sec(-1) for transformylase activity (at pH 8). kcat is 0.309 sec(-1) for acetate kinase activity (at pH 8).1 Publication
  1. KM=10.1 µM for GAR (at pH 8)2 Publications
  2. KM=45 µM for ATP (with formate)1 Publication
  3. KM=77.4 µM for ATP (with acetate at pH 8)2 Publications
  4. KM=319 µM for formate (at pH 8)2 Publications
  5. KM=3.68 mM for acetate (at pH 8)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route).UniRule annotation3 Publications This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei825'-phosphoribosylglycinamideUniRule annotation2 Publications1
Binding sitei114ATPUniRule annotation2 Publications1
Binding sitei155ATPUniRule annotation2 Publications1
Binding sitei203ATPUniRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi267MagnesiumUniRule annotation2 Publications1
Metal bindingi279MagnesiumUniRule annotation2 Publications1
Binding sitei2865'-phosphoribosylglycinamideUniRule annotation2 Publications1
Binding sitei3555'-phosphoribosylglycinamideUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi160 – 165ATPUniRule annotation2 Publications6
Nucleotide bindingi195 – 198ATPUniRule annotation2 Publications4

<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

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 functionLigase
Biological processPurine biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:GARTRANSFORMYL2-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P33221

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

More...
UniPathwayi
UPA00074;UER00127

<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%5Fand%5Ftaxonomy%5Fsection">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:
Formate-dependent phosphoribosylglycinamide formyltransferase1 Publication (EC:6.3.1.213 Publications)
Alternative name(s):
5'-phosphoribosylglycinamide transformylase 21 Publication
Formate-dependent GAR transformylase1 Publication
GAR transformylase 21 Publication
Short name:
GART 21 Publication
GAR transformylase T1 Publication
Non-folate glycinamide ribonucleotide transformylase1 Publication
Phosphoribosylglycinamide formyltransferase 21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:purT1 Publication
Ordered Locus Names:b1849, JW1838
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant defective in both purN and purT requires an exogenous purine source for growth.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi162G → I: Strong decrease in the reaction rate for the conversion of formate to FGAR and in the affinity for formate. 3- and 2-fold decrease in the affinity for ATP and GAR, respectively. 1 Publication1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:8653

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03434, 3-(N-morpholino)propanesulfonic acid
DB02930, Adenosine 5'-[gamma-thio]triphosphate
DB03909, Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate
DB02236, Glycinamide Ribonucleotide
DB04395, Phosphoaminophosphonic Acid-Adenylate Ester

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000749562 – 392Formate-dependent phosphoribosylglycinamide formyltransferaseAdd BLAST391

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 residuei179N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P33221

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

More...
PaxDbi
P33221

PRoteomics IDEntifications database

More...
PRIDEi
P33221

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P33221

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

UniRule annotation1 Publication2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260365, 7 interactors
850725, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-10618N

Protein interaction database and analysis system

More...
IntActi
P33221, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1849

<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

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P33221

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P33221

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini119 – 308ATP-graspUniRule annotationAdd BLAST190

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>Regioni22 – 235'-phosphoribosylglycinamide bindingUniRule annotation2 Publications2
Regioni362 – 3635'-phosphoribosylglycinamide bindingUniRule annotation2 Publications2

<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 PurK/PurT family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0027, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P33221

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P33221

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1490.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01643, PurT, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011761, ATP-grasp
IPR003135, ATP-grasp_carboxylate-amine
IPR013815, ATP_grasp_subdomain_1
IPR016185, PreATP-grasp_dom_sf
IPR005862, PurT
IPR011054, Rudment_hybrid_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02222, ATP-grasp, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01142, purT, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975, ATP_GRASP, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P33221-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM
60 70 80 90 100
HVAHRSHVIN MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN
110 120 130 140 150
VVPCARATKL TMNREGIRRL AAEELQLPTS TYRFADSESL FREAVADIGY
160 170 180 190 200
PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY AQQGGRAGAG RVIVEGVVKF
210 220 230 240 250
DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS PLALERAQEI
260 270 280 290 300
ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
310 320 330 340 350
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI
360 370 380 390
RLFGKPEIDG SRRLGVALAT AESVVDAIER AKHAAGQVKV QG
Length:392
Mass (Da):42,434
Last modified:January 23, 2007 - v3
<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:i276B3883E7403EA9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L20897 Genomic DNA Translation: AAA23861.1
U00096 Genomic DNA Translation: AAC74919.1
AP009048 Genomic DNA Translation: BAA15657.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A54227

NCBI Reference Sequences

More...
RefSeqi
NP_416363.1, NC_000913.3
WP_000173484.1, NZ_SSZK01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74919; AAC74919; b1849
BAA15657; BAA15657; BAA15657

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946368

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1838
eco:b1849

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.400

<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
L20897 Genomic DNA Translation: AAA23861.1
U00096 Genomic DNA Translation: AAC74919.1
AP009048 Genomic DNA Translation: BAA15657.1
PIRiA54227
RefSeqiNP_416363.1, NC_000913.3
WP_000173484.1, NZ_SSZK01000001.1

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
1EYZX-ray1.75A/B1-392[»]
1EZ1X-ray1.75A/B1-392[»]
1KJ8X-ray1.60A/B2-392[»]
1KJ9X-ray1.60A/B2-392[»]
1KJIX-ray1.60A/B2-392[»]
1KJJX-ray1.75A/B2-392[»]
1KJQX-ray1.05A/B2-392[»]
SMRiP33221
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260365, 7 interactors
850725, 2 interactors
DIPiDIP-10618N
IntActiP33221, 7 interactors
STRINGi511145.b1849

Chemistry databases

DrugBankiDB03434, 3-(N-morpholino)propanesulfonic acid
DB02930, Adenosine 5'-[gamma-thio]triphosphate
DB03909, Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate
DB02236, Glycinamide Ribonucleotide
DB04395, Phosphoaminophosphonic Acid-Adenylate Ester

PTM databases

iPTMnetiP33221

Proteomic databases

jPOSTiP33221
PaxDbiP33221
PRIDEiP33221

Genome annotation databases

EnsemblBacteriaiAAC74919; AAC74919; b1849
BAA15657; BAA15657; BAA15657
GeneIDi946368
KEGGiecj:JW1838
eco:b1849
PATRICifig|1411691.4.peg.400

Organism-specific databases

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

More...
EchoBASEi
EB1757

Phylogenomic databases

eggNOGiCOG0027, Bacteria
InParanoidiP33221
PhylomeDBiP33221

Enzyme and pathway databases

UniPathwayiUPA00074;UER00127
BioCyciEcoCyc:GARTRANSFORMYL2-MONOMER
SABIO-RKiP33221

Miscellaneous databases

EvolutionaryTraceiP33221
PHI-baseiPHI:8653

Protein Ontology

More...
PROi
PR:P33221

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
HAMAPiMF_01643, PurT, 1 hit
InterProiView protein in InterPro
IPR011761, ATP-grasp
IPR003135, ATP-grasp_carboxylate-amine
IPR013815, ATP_grasp_subdomain_1
IPR016185, PreATP-grasp_dom_sf
IPR005862, PurT
IPR011054, Rudment_hybrid_motif
PfamiView protein in Pfam
PF02222, ATP-grasp, 1 hit
SUPFAMiSSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit
TIGRFAMsiTIGR01142, purT, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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<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 nameiPURT_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: P33221
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 192 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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