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
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

BioCyciCJEJ192222:G1G1F-915-MONOMER
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:Cj0953c
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000000799 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001920791 – 510Bifunctional purine biosynthesis protein PurHAdd BLAST510

Proteomic databases

PaxDbiQ9PNY2
PRIDEiQ9PNY2

Interactioni

Protein-protein interaction databases

IntActiQ9PNY2, 1 interactor
STRINGi192222.Cj0953c

Structurei

Secondary structure

1510
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Helixi13 – 22Combined sources10
Beta strandi26 – 29Combined sources4
Helixi31 – 39Combined sources9
Beta strandi63 – 65Combined sources3
Helixi78 – 83Combined sources6
Beta strandi91 – 99Combined sources9
Helixi103 – 109Combined sources7
Helixi113 – 118Combined sources6
Helixi124 – 133Combined sources10
Turni134 – 137Combined sources4
Beta strandi139 – 141Combined sources3
Helixi144 – 146Combined sources3
Helixi147 – 155Combined sources9
Helixi161 – 190Combined sources30
Beta strandi196 – 209Combined sources14
Beta strandi211 – 213Combined sources3
Beta strandi218 – 225Combined sources8
Helixi226 – 230Combined sources5
Beta strandi232 – 236Combined sources5
Helixi240 – 253Combined sources14
Beta strandi261 – 266Combined sources6
Beta strandi269 – 275Combined sources7
Helixi279 – 287Combined sources9
Helixi291 – 294Combined sources4
Beta strandi298 – 305Combined sources8
Helixi307 – 313Combined sources7
Beta strandi319 – 326Combined sources8
Helixi328 – 332Combined sources5
Beta strandi341 – 344Combined sources4
Beta strandi346 – 349Combined sources4
Beta strandi356 – 362Combined sources7
Beta strandi365 – 370Combined sources6
Turni376 – 381Combined sources6
Beta strandi382 – 384Combined sources3
Beta strandi386 – 388Combined sources3
Helixi392 – 407Combined sources16
Beta strandi413 – 417Combined sources5
Beta strandi420 – 425Combined sources6
Beta strandi427 – 429Combined sources3
Helixi431 – 444Combined sources14
Beta strandi453 – 455Combined sources3
Helixi464 – 471Combined sources8
Beta strandi476 – 479Combined sources4
Helixi486 – 496Combined sources11
Beta strandi499 – 502Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4EHIX-ray2.28A/B1-510[»]
ProteinModelPortaliQ9PNY2
SMRiQ9PNY2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 142MGS-likePROSITE-ProRule annotationAdd BLAST142

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DC1 Bacteria
COG0138 LUCA
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.

Q9PNY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRALLSVSDK EGIVEFGKEL ENLGFEILST GGTFKLLKEN GIKVIEVSDF
60 70 80 90 100
TKSPELFEGR VKTLHPKIHG GILHKRSDEN HIKQAKENEI LGIDLVCVNL
110 120 130 140 150
YPFKKTTIMS DDFDEIIENI DIGGPAMIRS AAKNYKDVMV LCDPLDYEKV
160 170 180 190 200
IETLKKGQND ENFRLNLMIK AYEHTANYDA YIANYMNERF NGGFGASKFI
210 220 230 240 250
VGQKVFDTKY GENPHQKGAL YEFDAFFSAN FKALKGEASF NNLTDINAAL
260 270 280 290 300
NLASSFDKAP AIAIVKHGNP CGFAIKENLV QSYIHALKCD SVSAYGGVVA
310 320 330 340 350
INGTLDEALA NKINEIYVEV IIAANVDEKA LAVFEGKKRI KIFTQESPFL
360 370 380 390 400
IRSFDKYDFK HIDGGFVYQN SDEVGEDELK NAKLMSQREA SKEELKDLEI
410 420 430 440 450
AMKIAAFTKS NNVVYVKNGA MVAIGMGMTS RIDAAKAAIA KAKEMGLDLQ
460 470 480 490 500
GCVLASEAFF PFRDSIDEAS KVGVKAIVEP GGSIRDDEVV KAADEYGMAL
510
YFTGVRHFLH
Length:510
Mass (Da):56,402
Last modified:October 1, 2000 - v1
Checksum:i56F356F04B3A2092
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA Translation: CAL35073.1
PIRiH81369
RefSeqiWP_002853339.1, NC_002163.1
YP_002344351.1, NC_002163.1

Genome annotation databases

EnsemblBacteriaiCAL35073; CAL35073; Cj0953c
GeneIDi905247
KEGGicje:Cj0953c
PATRICifig|192222.6.peg.937

Similar proteinsi

Entry informationi

Entry nameiPUR9_CAMJE
AccessioniPrimary (citable) accession number: Q9PNY2
Secondary accession number(s): Q0P9U6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: October 1, 2000
Last modified: March 28, 2018
This is version 95 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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