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P08192 (FOLC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional protein FolC

Including the following 2 domains:

  1. Folylpolyglutamate synthase
    EC=6.3.2.17
    Alternative name(s):
    Folylpoly-gamma-glutamate synthetase
    Short name=FPGS
    Tetrahydrofolylpolyglutamate synthase
    Short name=Tetrahydrofolate synthase
  2. Dihydrofolate synthase
    EC=6.3.2.12
Gene names
Name:folC
Synonyms:dedC
Ordered Locus Names:b2315, JW2312
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conversion of folates to polyglutamate derivatives.

Catalytic activity

ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).

ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate.

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.

Subunit structure

Monomer.

Sequence similarities

Belongs to the folylpolyglutamate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Bifunctional protein FolC
PRO_0000168303

Regions

Nucleotide binding56 – 627ATP By similarity

Amino acid modifications

Disulfide bond354 ↔ 401 Probable

Experimental info

Sequence conflict3261V → M in AAA23808. Ref.1
Sequence conflict3261V → M in AAA23802. Ref.1
Sequence conflict3281A → AA in AAA23966. Ref.2
Sequence conflict391 – 3922DA → EP in AAA23966. Ref.2

Secondary structure

....................................................................... 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08192 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 0C0F33D3CFB77705

FASTA42245,406
        10         20         30         40         50         60 
MIIKRTPQAA SPLASWLSYL ENLHSKTIDL GLERVSLVAA RLGVLKPAPF VFTVAGTNGK 

        70         80         90        100        110        120 
GTTCRTLESI LMAAGYKVGV YSSPHLVRYT ERVRVQGQEL PESAHTASFA EIESARGDIS 

       130        140        150        160        170        180 
LTYFEYGTLS ALWLFKQAQL DVVILEVGLG GRLDATNIVD ADVAVVTSIA LDHTDWLGPD 

       190        200        210        220        230        240 
RESIGREKAG IFRSEKPAIV GEPEMPSTIA DVAQEKGALL QRRGVEWNYS VTDHDWAFSD 

       250        260        270        280        290        300 
AHGTLENLPL PLVPQPNAAT ALAALRASGL EVSENAIRDG IASAILPGRF QIVSESPRVI 

       310        320        330        340        350        360 
FDVAHNPHAA EYLTGRMKAL PKNGRVLAVI GMLHDKDIAG TLAWLKSVVD DWYCAPLEGP 

       370        380        390        400        410        420 
RGATAEQLLE HLGNGKSFDS VAQAWDAAMA DAKAEDTVLV CGSFHTVAHV MEVIDARRSG 


GK 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene."
Bognar A.L., Osborne C., Shane B.
J. Biol. Chem. 262:12337-12343(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons."
Nonet M.L., Marvel C.C., Tolan D.R.
J. Biol. Chem. 262:12209-12217(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli."
Kimlova L.J., Pyne C., Keshavjee K., Huy J., Beebakhee G., Bognar A.L.
Arch. Biochem. Biophys. 284:9-16(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRSYECFG. A65004.
RefSeqNP_416818.1. NC_000913.2.
YP_490557.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W78X-ray1.82A1-422[»]
1W7KX-ray2.10A1-422[»]
ProteinModelPortalP08192.
SMRP08192. Positions 6-419.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9674N.
IntActP08192. 9 interactions.
MINTMINT-1301447.
STRING511145.b2315.

Proteomic databases

PaxDbP08192.
PRIDEP08192.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75375; AAC75375; b2315.
BAA16164; BAA16164; BAA16164.
GeneID12932368.
945451.
KEGGecj:Y75_p2281.
eco:b2315.
PATRIC32120001. VBIEscCol129921_2410.

Organism-specific databases

EchoBASEEB0323.
EcoGeneEG10327. folC.

Phylogenomic databases

eggNOGCOG0285.
HOGENOMHOG000019982.
KOK11754.
OMAVIAIVEH.
ProtClustDBPRK10846.

Enzyme and pathway databases

BioCycEcoCyc:FOLC-MONOMER.
ECOL316407:JW2312-MONOMER.
MetaCyc:FOLC-MONOMER.
UniPathwayUPA00077; UER00157.

Gene expression databases

GenevestigatorP08192.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
InterProIPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
PANTHERPTHR11136. PTHR11136. 1 hit.
PfamPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
PIRSFPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01499. folC. 1 hit.
PROSITEPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01015. Sulfamethoxazole.
DB00440. Trimethoprim.
EvolutionaryTraceP08192.

Entry information

Entry nameFOLC_ECOLI
AccessionPrimary (citable) accession number: P08192
Secondary accession number(s): P78237
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families