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Entry version 167 (18 Sep 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Dihydrofolate synthase/folylpolyglutamate synthase

Gene

folC

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

Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.3 Publications

Miscellaneous

Mutant studies have shown that dihydrofolate synthase and folylpolyglutamate synthetase activities are catalyzed by a single catalytic site.2 Publications

<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

Mg2+1 PublicationNote: Binds 2 Mg2+ ions per subunit.1 Publication

<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 25 min(-1) with 7,8-dihydropteroate as substrate (at 30 degrees Celsius).1 Publication
  1. KM=0.6 µM for 7,8-dihydropteroate1 Publication
  2. KM=6.9 µM for ATP (in the assay for DHFS activity)1 Publication
  3. KM=3.9 mM for glutamate (in the assay for DHFS activity)1 Publication
  4. KM=0.6 µM for (6RS)-10-formyl-tetrahydropteroyl-gamma-Glu1 Publication
  5. KM=66.5 µM for ATP (in the assay for FPGS activity)1 Publication
  6. KM=333 µM for glutamate (in the assay for FPGS activity)1 Publication
  7. KM=0.9 µM for 7,8-dihydropteroate1 Publication
  8. KM=10 µM for ATP (in the assay for DHFS activity)1 Publication
  9. KM=2.8 mM for glutamate (in the assay for DHFS activity)1 Publication
  10. KM=17 µM for 10-formyl-tetrahydropteroyl-gamma-Glu1 Publication
  11. KM=54 µM for ATP (in the assay for FPGS activity)1 Publication
  12. KM=300 µM for glutamate (in the assay for FPGS activity)1 Publication
  13. KM=6.3 µM for 7,8-dihydropteroate1 Publication
  14. KM=50 µM for 5,10-methylenetetrahydrofolate1 Publication
  15. KM=50 µM for tetrahydrofolate1 Publication
  16. KM=1.4 µM for tetrahydrofolate diglutamate1 Publication
  1. Vmax=1.1 µmol/h/mg enzyme for DHFS activity1 Publication
  2. Vmax=4.1 µmol/h/mg enzyme for FPGS activity with 10-formyl-tetrahydropteroyl-gamma-Glu as substrate1 Publication
  3. Vmax=415 µmol/h/mg enzyme for FPGS activity with tetrahydrofolate as substrate1 Publication
  4. Vmax=380 µmol/h/mg enzyme for FPGS activity with tetrahydrofolate diglutamate as substrate1 Publication
  5. Vmax=13 µmol/h/mg enzyme for DHFS activity1 Publication

<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 biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Dihydropteroate synthase (folP), Dihydropteroate synthase (sul1), Dihydropteroate synthase (folP), Dihydropteroate synthase (sul2), Dihydropteroate synthase (sul2), Dihydropteroate synthase (folP)
  2. Dihydrofolate synthase/folylpolyglutamate synthase (folC)
This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Pathwayi: tetrahydrofolylpolyglutamate biosynthesis

This protein is involved in the pathway tetrahydrofolylpolyglutamate biosynthesis, which is part of Cofactor biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolylpolyglutamate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi83Magnesium 11 Publication1
Metal bindingi146Magnesium 11 Publication1
Metal bindingi173Magnesium 21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei257ATPCombined sources1 Publication1
Binding sitei289ATPCombined sources1 Publication1
Binding sitei302ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi59 – 62ATPCombined sources1 Publication4

<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

  • ATP binding Source: UniProtKB-KW
  • dihydrofolate synthase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • tetrahydrofolylpolyglutamate synthase activity Source: EcoCyc

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 processFolate biosynthesis, One-carbon metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:FOLC-MONOMER
ECOL316407:JW2312-MONOMER
MetaCyc:FOLC-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.2.17 2026

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

More...
UniPathwayi
UPA00077;UER00157
UPA00850

<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:
Dihydrofolate synthase/folylpolyglutamate synthaseCurated (EC:6.3.2.123 Publications, EC:6.3.2.171 Publication)
Short name:
DHFS / FPGS1 Publication
Alternative name(s):
Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase1 Publication
Folylpolyglutamate synthetase1 Publication
Tetrahydrofolylpolyglutamate synthase
<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:folC1 Publication
Synonyms:dedC
Ordered Locus Names:b2315, JW2312
<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
EG10327 folC

<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

  • cytoplasm Source: EcoCyc

<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>Mutagenesisi122T → H or W: Causes large decrease in affinity for both THF and DHP. 1 Publication1
Mutagenesisi154D → A: Severely impairs activity with THF as substrate, even more so than with DHP. Both substrates show a reduced affinity, but the catalytic rate with THF is 23-fold lower than wild-type, whereas that with DHP is 2.5-fold lower. The catalytic rate with THF diglutamate is 10-fold higher than with monoglutamate and close to that of the wild-type enzyme. 1 Publication1
Mutagenesisi155A → H: Causes large decrease in affinity for both THF and DHP. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3309008

Drug and drug target database

More...
DrugBanki
DB02437 (5r)-5-Amino-6-Hydroxyhexylcarbamic Acid
DB03830 Phosphorylated Dihydropteroate
DB01015 Sulfamethoxazole

<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_00001683031 – 422Dihydrofolate synthase/folylpolyglutamate synthaseAdd BLAST422

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 residuei188N6-carboxylysine1 Publication1

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P08192

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

More...
PaxDbi
P08192

PRoteomics IDEntifications database

More...
PRIDEi
P08192

<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

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261362, 413 interactors

Database of interacting proteins

More...
DIPi
DIP-9674N

Protein interaction database and analysis system

More...
IntActi
P08192, 10 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2315

<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

1422
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

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SMRi
P08192

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P08192

<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>Regioni29 – 317,8-dihydropteroate bindingCombined sources1 Publication3
Regioni122 – 1257,8-dihydropteroate bindingCombined sources1 Publication4
Regioni153 – 1557,8-dihydropteroate bindingCombined sources1 Publication3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal domain alone (residues 1-287) is sufficient to bind both tetrahydrofolate and dihydropteroate with the same affinity as the intact enzyme, but is not able to bind ATP and has no enzymatic activity.1 Publication

<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 folylpolyglutamate synthase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DPM Bacteria
COG0285 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000019982

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08192

KEGG Orthology (KO)

More...
KOi
K11754

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P08192

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1190.10, 1 hit
3.90.190.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001645 Folylpolyglutamate_synth
IPR018109 Folylpolyglutamate_synth_CS
IPR036565 Mur-like_cat_sf
IPR004101 Mur_ligase_C
IPR036615 Mur_ligase_C_dom_sf
IPR013221 Mur_ligase_cen

The PANTHER Classification System

More...
PANTHERi
PTHR11136 PTHR11136, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02875 Mur_ligase_C, 1 hit
PF08245 Mur_ligase_M, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001563 Folylpolyglu_synth, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01499 folC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01011 FOLYLPOLYGLU_SYNT_1, 1 hit
PS01012 FOLYLPOLYGLU_SYNT_2, 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>. 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_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.

P08192-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIIKRTPQAA SPLASWLSYL ENLHSKTIDL GLERVSLVAA RLGVLKPAPF
60 70 80 90 100
VFTVAGTNGK GTTCRTLESI LMAAGYKVGV YSSPHLVRYT ERVRVQGQEL
110 120 130 140 150
PESAHTASFA EIESARGDIS LTYFEYGTLS ALWLFKQAQL DVVILEVGLG
160 170 180 190 200
GRLDATNIVD ADVAVVTSIA LDHTDWLGPD RESIGREKAG IFRSEKPAIV
210 220 230 240 250
GEPEMPSTIA DVAQEKGALL QRRGVEWNYS VTDHDWAFSD AHGTLENLPL
260 270 280 290 300
PLVPQPNAAT ALAALRASGL EVSENAIRDG IASAILPGRF QIVSESPRVI
310 320 330 340 350
FDVAHNPHAA EYLTGRMKAL PKNGRVLAVI GMLHDKDIAG TLAWLKSVVD
360 370 380 390 400
DWYCAPLEGP RGATAEQLLE HLGNGKSFDS VAQAWDAAMA DAKAEDTVLV
410 420
CGSFHTVAHV MEVIDARRSG GK
Length:422
Mass (Da):45,406
Last modified:November 1, 1997 - v2
<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:i0C0F33D3CFB77705
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti326V → M in AAA23808 (PubMed:3040739).Curated1
Sequence conflicti326V → M in AAA23802 (PubMed:3040739).Curated1
Sequence conflicti328A → AA in AAA23966 (PubMed:3040734).Curated1
Sequence conflicti391 – 392DA → EP in AAA23966 (PubMed:3040734).Curated2

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
M32445 Genomic DNA Translation: AAA23808.1
J02808 Genomic DNA Translation: AAA23802.1
M68934 Genomic DNA Translation: AAA23966.1
U00096 Genomic DNA Translation: AAC75375.1
AP009048 Genomic DNA Translation: BAA16164.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A65004 SYECFG

NCBI Reference Sequences

More...
RefSeqi
NP_416818.1, NC_000913.3
WP_000584546.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75375; AAC75375; b2315
BAA16164; BAA16164; BAA16164

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945451

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2312
eco:b2315

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.2410

<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
M32445 Genomic DNA Translation: AAA23808.1
J02808 Genomic DNA Translation: AAA23802.1
M68934 Genomic DNA Translation: AAA23966.1
U00096 Genomic DNA Translation: AAC75375.1
AP009048 Genomic DNA Translation: BAA16164.1
PIRiA65004 SYECFG
RefSeqiNP_416818.1, NC_000913.3
WP_000584546.1, 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
1W78X-ray1.82A1-422[»]
1W7KX-ray2.10A1-422[»]
SMRiP08192
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4261362, 413 interactors
DIPiDIP-9674N
IntActiP08192, 10 interactors
STRINGi511145.b2315

Chemistry databases

ChEMBLiCHEMBL3309008
DrugBankiDB02437 (5r)-5-Amino-6-Hydroxyhexylcarbamic Acid
DB03830 Phosphorylated Dihydropteroate
DB01015 Sulfamethoxazole

DrugCentral

More...
DrugCentrali
P08192

Proteomic databases

jPOSTiP08192
PaxDbiP08192
PRIDEiP08192

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75375; AAC75375; b2315
BAA16164; BAA16164; BAA16164
GeneIDi945451
KEGGiecj:JW2312
eco:b2315
PATRICifig|511145.12.peg.2410

Organism-specific databases

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

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EchoBASEi
EB0323
EcoGeneiEG10327 folC

Phylogenomic databases

eggNOGiENOG4105DPM Bacteria
COG0285 LUCA
HOGENOMiHOG000019982
InParanoidiP08192
KOiK11754
PhylomeDBiP08192

Enzyme and pathway databases

UniPathwayiUPA00077;UER00157
UPA00850
BioCyciEcoCyc:FOLC-MONOMER
ECOL316407:JW2312-MONOMER
MetaCyc:FOLC-MONOMER
BRENDAi6.3.2.17 2026

Miscellaneous databases

EvolutionaryTraceiP08192

Protein Ontology

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PROi
PR:P08192

Family and domain databases

Gene3Di3.40.1190.10, 1 hit
3.90.190.20, 1 hit
InterProiView protein in InterPro
IPR001645 Folylpolyglutamate_synth
IPR018109 Folylpolyglutamate_synth_CS
IPR036565 Mur-like_cat_sf
IPR004101 Mur_ligase_C
IPR036615 Mur_ligase_C_dom_sf
IPR013221 Mur_ligase_cen
PANTHERiPTHR11136 PTHR11136, 1 hit
PfamiView protein in Pfam
PF02875 Mur_ligase_C, 1 hit
PF08245 Mur_ligase_M, 1 hit
PIRSFiPIRSF001563 Folylpolyglu_synth, 1 hit
SUPFAMiSSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit
TIGRFAMsiTIGR01499 folC, 1 hit
PROSITEiView protein in PROSITE
PS01011 FOLYLPOLYGLU_SYNT_1, 1 hit
PS01012 FOLYLPOLYGLU_SYNT_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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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 nameiFOLC_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: P08192
Secondary accession number(s): P78237
<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: August 1, 1988
Last sequence update: November 1, 1997
Last modified: September 18, 2019
This is version 167 of the entry and version 2 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, 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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