Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Escherichia coli 5-366-08_S1_C1
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotationSAAS annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotationSAAS annotation

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route).UniRule annotationSAAS annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PurH (purH)
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 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotationSAAS annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PurH (purH)
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 IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotationSAAS annotationImported, Multifunctional enzymeUniRule annotationSAAS annotation, TransferaseUniRule annotationSAAS annotationImported
Biological processPurine biosynthesisUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133
UPA00074; UER00135

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurHUniRule annotation
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
Alternative name(s):
AICAR transformylaseUniRule annotation
IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
Alternative name(s):
ATICUniRule annotation
IMP synthaseUniRule annotation
InosinicaseUniRule annotation
Gene namesi
Name:purHUniRule annotationImported
ORF Names:AB08_4910Imported
OrganismiEscherichia coli 5-366-08_S1_C1Imported
Taxonomic identifieri1444047 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000027710 Componenti: Unassembled WGS sequence

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei287N6-acetyllysineUniRule annotation1

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA0A073UTI7
SMRiA0A073UTI7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 132MGSInterPro annotationAdd BLAST114

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.UniRule annotationSAAS annotation

Family and domain databases

Gene3Di3.40.140.20, 2 hits
3.40.50.1380, 1 hit
HAMAPiMF_00139 PurH, 1 hit
InterProiView protein in InterPro
IPR024051 AICAR_Tfase_dup_dom_sf
IPR016193 Cytidine_deaminase-like
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR002695 PurH-like
PANTHERiPTHR11692 PTHR11692, 1 hit
PfamiView protein in Pfam
PF01808 AICARFT_IMPCHas, 1 hit
PF02142 MGS, 1 hit
PIRSFiPIRSF000414 AICARFT_IMPCHas, 1 hit
SMARTiView protein in SMART
SM00798 AICARFT_IMPCHas, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF52335 SSF52335, 1 hit
SSF53927 SSF53927, 1 hit
TIGRFAMsiTIGR00355 purH, 1 hit

Sequencei

Sequence statusi: Complete.

A0A073UTI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQRRPVRRA LLSVSDKAGI VEFAQALSAR GVELLSTGGT ARLLAEKGLP
60 70 80 90 100
VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EEHQIQPIDM
110 120 130 140 150
VVVNLYPFAQ TVAREGCSLE DAVENIDIGG PTMVRSAAKN HKDVAIVVKS
160 170 180 190 200
SDYDAIIKEM DDNEGSLTLA TRFDLAIKAF EHTAAYDSMI ANYFGSMVPA
210 220 230 240 250
YHGESKEAAG RFPRTLNLNF IKKQDMRYGE NSHQQAAFYI EENVKEASVA
260 270 280 290 300
TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI
310 320 330 340 350
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE
360 370 380 390 400
EALKITAAKQ NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE
410 420 430 440 450
LRVVTKRQPT EQELRDALFC WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR
460 470 480 490 500
VYSAKIAGIK AADEGLEVKG SSMASDAFFP FRDGIDAAAA AGVTCVIQPG
510 520
GSIRDDEVIA AADEHGIAML FTDMRHFRH
Length:529
Mass (Da):57,358
Last modified:October 1, 2014 - v1
Checksum:iF0FDD9FB71CAB1B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JOQU01000043 Genomic DNA Translation: KEL65274.1
RefSeqiWP_001187564.1, NZ_JOQU01000043.1

Genome annotation databases

EnsemblBacteriaiKEL65274; KEL65274; AB08_4910
PATRICifig|1444047.3.peg.4754

Entry informationi

Entry nameiA0A073UTI7_ECOLX
AccessioniPrimary (citable) accession number: A0A073UTI7
Entry historyiIntegrated into UniProtKB/TrEMBL: October 1, 2014
Last sequence update: October 1, 2014
Last modified: June 20, 2018
This is version 27 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health