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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Clostridium perfringens (strain 13 / 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

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
Ordered Locus Names:CPE0686
OrganismiClostridium perfringens (strain 13 / Type A)
Taxonomic identifieri195102 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000818 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001920851 – 501Bifunctional purine biosynthesis protein PurHAdd BLAST501

Structurei

3D structure databases

ProteinModelPortaliQ8XMK2
SMRiQ8XMK2
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
OrthoDBiPOG091H00UT

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.

Q8XMK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRALISVF DKDGVLELAK FLRDRDVEII SSGGTYKYLK ENNIEVKEIS
60 70 80 90 100
EITDFPEMLD GRVKTLHPLV HAGILAIRDN KEHMKTLEER EINTIDYVVV
110 120 130 140 150
NLYPFFEKVR EDLSFEEKVE 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 VVTEKEPTEM ELRDMIFGMK
410 420 430 440 450
VVKYVKSNAI VVVKDGVATG IGGGQVNRIW ATKEALERGK GGAVLASDAF
460 470 480 490 500
FPFRDCVDEA AKNGIKAIIQ PGGSIRDEES IEACNEHGIS MVFTGVRHFK

H
Length:501
Mass (Da):56,125
Last modified:March 1, 2002 - v1
Checksum:i611E1062B2BA10CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000016 Genomic DNA Translation: BAB80392.1
RefSeqiWP_011009972.1, NC_003366.1

Genome annotation databases

EnsemblBacteriaiBAB80392; BAB80392; BAB80392
KEGGicpe:CPE0686

Similar proteinsi

Entry informationi

Entry nameiPUR9_CLOPE
AccessioniPrimary (citable) accession number: Q8XMK2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2002
Last modified: March 28, 2018
This is version 92 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, Reference proteome
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Main funding by: National Institutes of Health