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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Shigella flexneri 1235-66
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), 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), 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 annotation, 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 annotation
ORF Names:SF123566_5963Imported
OrganismiShigella flexneri 1235-66Imported
Taxonomic identifieri766154 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella

PTM / Processingi

Amino acid modifications

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

Keywords - PTMi

AcetylationUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliI6G867
SMRiI6G867
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

Phylogenomic databases

OMAiDLLFAWK

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.

I6G867-1 [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
LRVVTQRQPT 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:September 5, 2012 - v1
Checksum:iF0E839F491D0B1B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AKNF01001054 Genomic DNA Translation: EIQ64709.1

Genome annotation databases

EnsemblBacteriaiEIQ64709; EIQ64709; SF123566_5963
PATRICifig|766154.3.peg.7711

Entry informationi

Entry nameiI6G867_SHIFL
AccessioniPrimary (citable) accession number: I6G867
Entry historyiIntegrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: June 20, 2018
This is version 42 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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