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Protein

5-formyltetrahydrofolate cyclo-ligase

Gene

ygfA

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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) (By similarity).By similarity

Catalytic activityi

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

Pathwayi: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3751-MONOMER.
ECOO157:YGFA-MONOMER.
UniPathwayiUPA00193.

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:Z4249, ECs3782
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1821825-formyltetrahydrofolate cyclo-ligasePRO_0000200285Add
BLAST

Interactioni

Protein-protein interaction databases

MINTiMINT-1249433.
STRINGi155864.Z4249.

Structurei

3D structure databases

ProteinModelPortaliP0AC29.
SMRiP0AC29. Positions 8-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

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.

P0AC29-1 [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
AE005174 Genomic DNA. Translation: AAG58038.1.
BA000007 Genomic DNA. Translation: BAB37205.1.
PIRiF91101.
RefSeqiNP_311809.3. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG58038; AAG58038; Z4249.
BAB37205; BAB37205; BAB37205.
GeneIDi916397.
KEGGiece:Z4249.
ecs:ECs3782.
PATRICi18357051. VBIEscCol44059_3704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG58038.1.
BA000007 Genomic DNA. Translation: BAB37205.1.
PIRiF91101.
RefSeqiNP_311809.3. NC_002695.1.

3D structure databases

ProteinModelPortaliP0AC29.
SMRiP0AC29. Positions 8-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1249433.
STRINGi155864.Z4249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG58038; AAG58038; Z4249.
BAB37205; BAB37205; BAB37205.
GeneIDi916397.
KEGGiece:Z4249.
ecs:ECs3782.
PATRICi18357051. VBIEscCol44059_3704.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciECOL386585:GJFA-3751-MONOMER.
ECOO157:YGFA-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry namei5FCL_ECO57
AccessioniPrimary (citable) accession number: P0AC29
Secondary accession number(s): P09160
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: November 11, 2015
This is version 58 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.