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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Clostridium perfringens (strain SM101 / Type A)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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 annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule 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 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 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 functionHydrolase, Multifunctional enzyme, Transferase
Biological processPurine biosynthesis

Enzyme and pathway databases

UniPathwayi
UPA00074;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
Ordered Locus Names:CPR_0675
OrganismiClostridium perfringens (strain SM101 / Type A)
Taxonomic identifieri289380 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000001824 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000188811 – 501Bifunctional purine biosynthesis protein PurHAdd BLAST501

Structurei

3D structure databases

ProteinModelPortaliQ0SV48
SMRiQ0SV48
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 144MGS-likePROSITE-ProRule annotationAdd BLAST144

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000230373
KOiK00602
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
PROSITEiView protein in PROSITE
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

Q0SV48-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKRALISVF DKDGVLELAK FLRDRDVEII SSGGTYKYLK ENNIEVKEIS
60 70 80 90 100
EITDFPEMLD GRVKTLHPLV HAGILAIRDN KEHMKTLEKR EINTIDYVVV
110 120 130 140 150
NLYPFFEKVR ENLSFEEKVE FIDIGGPTML RAAAKNFKDV VVLSDKKDYE
160 170 180 190 200
KVMNEIKENN CVSFKLRKTL AGKVFNLMSA YDAAISNFLL EGEEEYPEYL
210 220 230 240 250
SVSYKKIQDL RYGENPHQGA AYYSSTEFDG AMNSFEILNG KALSYNNIKD
260 270 280 290 300
LDIAWKVACE FEETACCALK HNTPCGVAVG ENSKEVYLKA YDADPVSIFG
310 320 330 340 350
GIVAINRKID KATAEEMVKI FLEVVAAPDF DEDALEVLRT KKNLRVIKCK
360 370 380 390 400
NTPQAKNYMV TVDGGILVQG EDNKLANEYK VVTKKEPTEM ELRDMIFGMK
410 420 430 440 450
VVKYVKSNAI VVVKDGVATG IGGGQVNRIW ATKEALERGK GGAVLASDAF
460 470 480 490 500
FPFRDCVDEA AKNGIKAIIQ PGGSIRDEES VEACNEHGIS MVFTGVRHFK

H
Length:501
Mass (Da):56,108
Last modified:September 5, 2006 - v1
Checksum:iBE889F267E4A911D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000312 Genomic DNA Translation: ABG87320.1

Genome annotation databases

EnsemblBacteriaiABG87320; ABG87320; CPR_0675
KEGGicpr:CPR_0675

Similar proteinsi

Entry informationi

Entry nameiPUR9_CLOPS
AccessioniPrimary (citable) accession number: Q0SV48
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: March 28, 2018
This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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