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Protein

Formyltetrahydrofolate deformylase

Gene

purU

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

Functioni

Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). Provides the major source of formate for the PurT-dependent synthesis of 5'-phosphoribosyl-N-formylglycinamide (FGAR) during aerobic growth. Has a role in regulating the one-carbon pool.UniRule annotation1 Publication

Catalytic activityi

10-formyltetrahydrofolate + H2O = formate + tetrahydrofolate.UniRule annotation1 Publication

Enzyme regulationi

Activated by methionine, inhibited by glycine.1 Publication

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes formate from 10-formyl-5,6,7,8-tetrahydrofolate.UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Formyltetrahydrofolate deformylase (purU)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes formate from 10-formyl-5,6,7,8-tetrahydrofolate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei225UniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
  • 10-formyltetrahydrofolate biosynthetic process Source: EcoCyc
  • one-carbon metabolic process Source: EcoCyc
  • purine nucleotide biosynthetic process Source: CACAO
  • purine ribonucleotide biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism, Purine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:FORMYLTHFDEFORMYL-MONOMER.
ECOL316407:JW1220-MONOMER.
MetaCyc:FORMYLTHFDEFORMYL-MONOMER.
UniPathwayiUPA00074; UER00170.

Names & Taxonomyi

Protein namesi
Recommended name:
Formyltetrahydrofolate deformylaseUniRule annotation (EC:3.5.1.10UniRule annotation)
Alternative name(s):
Formyl-FH(4) hydrolaseUniRule annotation
Gene namesi
Name:purUUniRule annotation
Synonyms:tgs, ychI
Ordered Locus Names:b1232, JW1220
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11819. purU.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000749611 – 280Formyltetrahydrofolate deformylaseAdd BLAST280

Proteomic databases

EPDiP37051.
PaxDbiP37051.
PRIDEiP37051.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

BioGridi4261924. 11 interactors.
IntActiP37051. 3 interactors.
STRINGi511145.b1232.

Structurei

3D structure databases

ProteinModelPortaliP37051.
SMRiP37051.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini8 – 86ACTUniRule annotationAdd BLAST79

Sequence similaritiesi

Belongs to the PurU family.UniRule annotation
Contains 1 ACT domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CIY. Bacteria.
COG0788. LUCA.
HOGENOMiHOG000033576.
InParanoidiP37051.
KOiK01433.
OMAiILRTICP.
PhylomeDBiP37051.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
HAMAPiMF_01927. PurU. 1 hit.
InterProiIPR002912. ACT_dom.
IPR002376. Formyl_transf_N.
IPR004810. PurU.
[Graphical view]
PANTHERiPTHR10520:SF7. PTHR10520:SF7. 1 hit.
PfamiPF01842. ACT. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
PRINTSiPR01575. FFH4HYDRLASE.
SUPFAMiSSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00655. PurU. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37051-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSLQRKVLR TICPDQKGLI ARITNICYKH ELNIVQNNEF VDHRTGRFFM
60 70 80 90 100
RTELEGIFND STLLADLDSA LPEGSVRELN PAGRRRIVIL VTKEAHCLGD
110 120 130 140 150
LLMKANYGGL DVEIAAVIGN HDTLRSLVER FDIPFELVSH EGLTRNEHDQ
160 170 180 190 200
KMADAIDAYQ PDYVVLAKYM RVLTPEFVAR FPNKIINIHH SFLPAFIGAR
210 220 230 240 250
PYHQAYERGV KIIGATAHYV NDNLDEGPII MQDVIHVDHT YTAEDMMRAG
260 270 280
RDVEKNVLSR ALYKVLAQRV FVYGNRTIIL
Length:280
Mass (Da):31,935
Last modified:June 1, 1994 - v1
Checksum:i5667406D2727A2C2
GO

Sequence cautioni

The sequence AAA16860 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20251 Unassigned DNA. Translation: AAC36846.1.
M64675 Unassigned DNA. Translation: AAA16860.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74314.1.
AP009048 Genomic DNA. Translation: BAA36100.1.
PIRiC36871.
RefSeqiNP_415748.1. NC_000913.3.
WP_000555857.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74314; AAC74314; b1232.
BAA36100; BAA36100; BAA36100.
GeneIDi945827.
KEGGiecj:JW1220.
eco:b1232.
PATRICi32117720. VBIEscCol129921_1280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20251 Unassigned DNA. Translation: AAC36846.1.
M64675 Unassigned DNA. Translation: AAA16860.1. Different initiation.
U00096 Genomic DNA. Translation: AAC74314.1.
AP009048 Genomic DNA. Translation: BAA36100.1.
PIRiC36871.
RefSeqiNP_415748.1. NC_000913.3.
WP_000555857.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP37051.
SMRiP37051.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261924. 11 interactors.
IntActiP37051. 3 interactors.
STRINGi511145.b1232.

Proteomic databases

EPDiP37051.
PaxDbiP37051.
PRIDEiP37051.

Protocols and materials databases

DNASUi945827.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74314; AAC74314; b1232.
BAA36100; BAA36100; BAA36100.
GeneIDi945827.
KEGGiecj:JW1220.
eco:b1232.
PATRICi32117720. VBIEscCol129921_1280.

Organism-specific databases

EchoBASEiEB1766.
EcoGeneiEG11819. purU.

Phylogenomic databases

eggNOGiENOG4105CIY. Bacteria.
COG0788. LUCA.
HOGENOMiHOG000033576.
InParanoidiP37051.
KOiK01433.
OMAiILRTICP.
PhylomeDBiP37051.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00170.
BioCyciEcoCyc:FORMYLTHFDEFORMYL-MONOMER.
ECOL316407:JW1220-MONOMER.
MetaCyc:FORMYLTHFDEFORMYL-MONOMER.

Miscellaneous databases

PROiP37051.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
HAMAPiMF_01927. PurU. 1 hit.
InterProiIPR002912. ACT_dom.
IPR002376. Formyl_transf_N.
IPR004810. PurU.
[Graphical view]
PANTHERiPTHR10520:SF7. PTHR10520:SF7. 1 hit.
PfamiPF01842. ACT. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
PRINTSiPR01575. FFH4HYDRLASE.
SUPFAMiSSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00655. PurU. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPURU_ECOLI
AccessioniPrimary (citable) accession number: P37051
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 136 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, Direct protein sequencing, 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. 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.