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Protein

Bifunctional protein FolC

Gene

folC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of folates to polyglutamate derivatives.

Catalytic activityi

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.

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.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Dihydropteroate synthase (folP)
  2. Bifunctional protein FolC (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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 627ATPBy similarity

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Folate biosynthesis, One-carbon metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein FolC
Including the following 2 domains:
Folylpolyglutamate synthase (EC:6.3.2.17)
Alternative name(s):
Folylpoly-gamma-glutamate synthetase
Short name:
FPGS
Tetrahydrofolylpolyglutamate synthase
Short name:
Tetrahydrofolate synthase
Dihydrofolate synthase (EC:6.3.2.12)
Gene namesi
Name:folC
Synonyms:dedC
Ordered Locus Names:b2315, JW2312
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10327. folC.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB01015. Sulfamethoxazole.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Bifunctional protein FolCPRO_0000168303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi354 ↔ 401Curated

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP08192.
PRIDEiP08192.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4261362. 387 interactions.
DIPiDIP-9674N.
IntActiP08192. 9 interactions.
MINTiMINT-1301447.
STRINGi511145.b2315.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 208Combined sources
Beta strandi23 – 275Combined sources
Helixi33 – 4210Combined sources
Beta strandi48 – 558Combined sources
Helixi60 – 7314Combined sources
Beta strandi78 – 814Combined sources
Helixi89 – 924Combined sources
Beta strandi93 – 953Combined sources
Helixi102 – 11514Combined sources
Turni116 – 1183Combined sources
Helixi123 – 13816Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi148 – 1514Combined sources
Helixi155 – 1584Combined sources
Beta strandi162 – 1665Combined sources
Helixi174 – 1774Combined sources
Helixi181 – 1888Combined sources
Helixi189 – 1913Combined sources
Beta strandi196 – 2005Combined sources
Helixi207 – 21610Combined sources
Beta strandi219 – 2235Combined sources
Turni224 – 2263Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi243 – 2486Combined sources
Helixi255 – 26814Combined sources
Helixi274 – 28310Combined sources
Beta strandi289 – 2946Combined sources
Turni295 – 2973Combined sources
Beta strandi298 – 3025Combined sources
Helixi307 – 31913Combined sources
Beta strandi326 – 3305Combined sources
Helixi338 – 3469Combined sources
Beta strandi350 – 3545Combined sources
Beta strandi359 – 3624Combined sources
Helixi365 – 3728Combined sources
Helixi381 – 39111Combined sources
Beta strandi397 – 4037Combined sources
Helixi404 – 41714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W78X-ray1.82A1-422[»]
1W7KX-ray2.10A1-422[»]
ProteinModelPortaliP08192.
SMRiP08192. Positions 6-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08192.

Family & Domainsi

Sequence similaritiesi

Belongs to the folylpolyglutamate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105DPM. Bacteria.
COG0285. LUCA.
HOGENOMiHOG000019982.
InParanoidiP08192.
KOiK11754.
OMAiFHALENI.
OrthoDBiEOG6ZPSW2.
PhylomeDBiP08192.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
InterProiIPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
PANTHERiPTHR11136. PTHR11136. 1 hit.
PfamiPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
PIRSFiPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsiTIGR01499. folC. 1 hit.
PROSITEiPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i0C0F33D3CFB77705
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti326 – 3261V → M in AAA23808 (PubMed:3040739).Curated
Sequence conflicti326 – 3261V → M in AAA23802 (PubMed:3040739).Curated
Sequence conflicti328 – 3281A → AA in AAA23966 (PubMed:3040734).Curated
Sequence conflicti391 – 3922DA → EP in AAA23966 (PubMed:3040734).Curated

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.

Genome annotation databases

EnsemblBacteriaiAAC75375; AAC75375; b2315.
BAA16164; BAA16164; BAA16164.
GeneIDi945451.
KEGGiecj:JW2312.
eco:b2315.
PATRICi32120001. VBIEscCol129921_2410.

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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W78X-ray1.82A1-422[»]
1W7KX-ray2.10A1-422[»]
ProteinModelPortaliP08192.
SMRiP08192. Positions 6-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261362. 387 interactions.
DIPiDIP-9674N.
IntActiP08192. 9 interactions.
MINTiMINT-1301447.
STRINGi511145.b2315.

Chemistry

DrugBankiDB01015. Sulfamethoxazole.

Proteomic databases

PaxDbiP08192.
PRIDEiP08192.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75375; AAC75375; b2315.
BAA16164; BAA16164; BAA16164.
GeneIDi945451.
KEGGiecj:JW2312.
eco:b2315.
PATRICi32120001. VBIEscCol129921_2410.

Organism-specific databases

EchoBASEiEB0323.
EcoGeneiEG10327. folC.

Phylogenomic databases

eggNOGiENOG4105DPM. Bacteria.
COG0285. LUCA.
HOGENOMiHOG000019982.
InParanoidiP08192.
KOiK11754.
OMAiFHALENI.
OrthoDBiEOG6ZPSW2.
PhylomeDBiP08192.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP08192.
PROiP08192.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
InterProiIPR001645. Folylpolyglutamate_synth.
IPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]
PANTHERiPTHR11136. PTHR11136. 1 hit.
PfamiPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
PIRSFiPIRSF001563. Folylpolyglu_synth. 1 hit.
SUPFAMiSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsiTIGR01499. folC. 1 hit.
PROSITEiPS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiFOLC_ECOLI
AccessioniPrimary (citable) accession number: P08192
Secondary accession number(s): P78237
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.