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Protein

5-formyltetrahydrofolate cyclo-ligase

Gene

ygfA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the removal of 5-formyltetrahydrofolate. In vitro, it is a potent inhibitor of various folate-dependent enzymes in the C1 metabolism network and in vivo it might function as a folate storage. 5-formyltetrahydrofolate is also used as an antifolate rescue agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10-methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is catalyzed by the serine hydroxymethyltransferase GlyA (SHMT).2 Publications

Catalytic activityi

ATP + 5-formyltetrahydrofolate = ADP + phosphate + 5,10-methenyltetrahydrofolate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671ATPSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1358ATPSequence analysis

GO - Molecular functioni

  • 5-formyltetrahydrofolate cyclo-ligase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • dormancy process Source: EcoCyc
  • folic acid-containing compound biosynthetic process Source: GO_Central
  • tetrahydrofolate interconversion Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11158-MONOMER.
ECOL316407:JW2879-MONOMER.
MetaCyc:EG11158-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
5-formyltetrahydrofolate cyclo-ligase (EC:6.3.3.2)
Short name:
5-FCL
Alternative name(s):
5,10-methenyltetrahydrofolate synthetase
Short name:
MTHFS
Gene namesi
Name:ygfA
Ordered Locus Names:b2912, JW2879
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11158. ygfA.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene does not cause a growth defect in rich or minimal medium. However, when grown in minimal medium with added glycine, the mutant accumulates 5-CHO-THF. If the only nitrogen source in minimal medium is glycine, the mutant shows a severe growth defect, likely due to inhibition of serine hydroxymethyltransferase (SHMT) and the glycine cleavage system by the accumulated 5-CHO-THF. This phenotype can be complemented by the glutamate formiminotransferase (FT).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1821825-formyltetrahydrofolate cyclo-ligasePRO_0000200284Add
BLAST

Proteomic databases

PaxDbiP0AC28.

Expressioni

Inductioni

During biofilm formation.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ndkP0A7633EBI-555094,EBI-370139

Protein-protein interaction databases

BioGridi4261171. 226 interactions.
DIPiDIP-48194N.
IntActiP0AC28. 9 interactions.
MINTiMINT-1249443.
STRINGi511145.b2912.

Structurei

3D structure databases

ProteinModelPortaliP0AC28.
SMRiP0AC28. Positions 8-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105MK2. Bacteria.
COG0212. LUCA.
HOGENOMiHOG000007300.
InParanoidiP0AC28.
KOiK01934.
OMAiFREWRAG.
OrthoDBiEOG6RVG1P.
PhylomeDBiP0AC28.

Family and domain databases

Gene3Di3.40.50.10420. 1 hit.
InterProiIPR002698. FTHF_cligase.
IPR024185. FTHF_cligase-like.
[Graphical view]
PANTHERiPTHR23407:SF1. PTHR23407:SF1. 1 hit.
PfamiPF01812. 5-FTHF_cyc-lig. 1 hit.
[Graphical view]
PIRSFiPIRSF006806. FTHF_cligase. 1 hit.
TIGRFAMsiTIGR02727. MTHFS_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AC28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRQRRRALT PEQQQEMGQQ AATRMMTYPP VVMAHTVAVF LSFDGELDTQ
60 70 80 90 100
PLIEQLWRAG KRVYLPVLHP FSAGNLLFLN YHPQSELVMN RLKIHEPKLD
110 120 130 140 150
VRDVLPLSRL DVLITPLVAF DEYGQRLGMG GGFYDRTLQN WQHYKTQPVG
160 170 180
YAHDCQLVEK LPVEEWDIPL PAVVTPSKVW EW
Length:182
Mass (Da):21,105
Last modified:November 8, 2005 - v1
Checksum:i389B13098552BF81
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12965 Genomic DNA. Translation: AAA24651.1.
U28377 Genomic DNA. Translation: AAA69079.1.
U00096 Genomic DNA. Translation: AAC75949.1.
AP009048 Genomic DNA. Translation: BAE76976.1.
PIRiA21894. QQEC2K.
RefSeqiNP_417387.3. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75949; AAC75949; b2912.
BAE76976; BAE76976; BAE76976.
GeneIDi945167.
KEGGiecj:JW2879.
eco:b2912.
PATRICi32121236. VBIEscCol129921_3006.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12965 Genomic DNA. Translation: AAA24651.1.
U28377 Genomic DNA. Translation: AAA69079.1.
U00096 Genomic DNA. Translation: AAC75949.1.
AP009048 Genomic DNA. Translation: BAE76976.1.
PIRiA21894. QQEC2K.
RefSeqiNP_417387.3. NC_000913.3.

3D structure databases

ProteinModelPortaliP0AC28.
SMRiP0AC28. Positions 8-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261171. 226 interactions.
DIPiDIP-48194N.
IntActiP0AC28. 9 interactions.
MINTiMINT-1249443.
STRINGi511145.b2912.

Proteomic databases

PaxDbiP0AC28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75949; AAC75949; b2912.
BAE76976; BAE76976; BAE76976.
GeneIDi945167.
KEGGiecj:JW2879.
eco:b2912.
PATRICi32121236. VBIEscCol129921_3006.

Organism-specific databases

EchoBASEiEB1147.
EcoGeneiEG11158. ygfA.

Phylogenomic databases

eggNOGiENOG4105MK2. Bacteria.
COG0212. LUCA.
HOGENOMiHOG000007300.
InParanoidiP0AC28.
KOiK01934.
OMAiFREWRAG.
OrthoDBiEOG6RVG1P.
PhylomeDBiP0AC28.

Enzyme and pathway databases

BioCyciEcoCyc:EG11158-MONOMER.
ECOL316407:JW2879-MONOMER.
MetaCyc:EG11158-MONOMER.

Miscellaneous databases

PROiP0AC28.

Family and domain databases

Gene3Di3.40.50.10420. 1 hit.
InterProiIPR002698. FTHF_cligase.
IPR024185. FTHF_cligase-like.
[Graphical view]
PANTHERiPTHR23407:SF1. PTHR23407:SF1. 1 hit.
PfamiPF01812. 5-FTHF_cyc-lig. 1 hit.
[Graphical view]
PIRSFiPIRSF006806. FTHF_cligase. 1 hit.
TIGRFAMsiTIGR02727. MTHFS_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli 6S RNA gene is part of a dual-function transcription unit."
    Hsu L.M., Zagorski J., Wang Z., Fournier M.J.
    J. Bacteriol. 161:1162-1170(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Role of global regulators and nucleotide metabolism in antibiotic tolerance in Escherichia coli."
    Hansen S., Lewis K., Vulic M.
    Antimicrob. Agents Chemother. 52:2718-2726(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Moonlighting glutamate formiminotransferases can functionally replace 5-formyltetrahydrofolate cycloligase."
    Jeanguenin L., Lara-Nunez A., Pribat A., Mageroy M.H., Gregory J.F. III, Rice K.C., de Crecy-Lagard V., Hanson A.D.
    J. Biol. Chem. 285:41557-41566(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Rho-dependent termination of ssrS (6S RNA) transcription in Escherichia coli: implication for 3' processing of 6S RNA and expression of downstream ygfA (putative 5-formyl-tetrahydrofolate cyclo-ligase)."
    Chae H., Han K., Kim K.S., Park H., Lee J., Lee Y.
    J. Biol. Chem. 286:114-122(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry namei5FCL_ECOLI
AccessioniPrimary (citable) accession number: P0AC28
Secondary accession number(s): P09160, Q2M9T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 13, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.