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
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
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:PC1_0225
OrganismiPectobacterium carotovorum subsp. carotovorum (strain PC1)
Taxonomic identifieri561230 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesPectobacteriaceaePectobacterium
Proteomesi
  • UP000002736 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002032521 – 529Bifunctional purine biosynthesis protein PurHAdd BLAST529

Proteomic databases

PRIDEiC6DHT5

Interactioni

Protein-protein interaction databases

STRINGi561230.PC1_0225

Structurei

3D structure databases

ProteinModelPortaliC6DHT5
SMRiC6DHT5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 148MGS-likePROSITE-ProRule annotationAdd BLAST148

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
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
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
TIGRFAMsiTIGR00355 purH, 1 hit
PROSITEiView protein in PROSITE
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

C6DHT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQRRPIRRA LLSVSDKAGI VEFAQALSHR GVELLSTGGT ARLLADAGLA
60 70 80 90 100
VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRDQDDAIM AQHDIKPIDI
110 120 130 140 150
VVVNLYPFAQ TVARENCTLE DAVENIDIGG PTMVRSAAKN HKDVAIVVKS
160 170 180 190 200
SDYSAIINEI DANEGSLTYE TRFDLAIKAF EHTAAYDSMI ANYFGALVPP
210 220 230 240 250
YHGETDKPSG NFPRTLNLNY IKKQDMRYGE NSHQQAAFYI EENIHEASVA
260 270 280 290 300
TSTQLQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PSGVAIGGSI
310 320 330 340 350
LDAYERAYKT DPTSAFGGII AFNRELDEET AQAIISRQFV EVIIAPSASE
360 370 380 390 400
AALKVTAAKQ NVRVLTSGNW QQRVPGLDFK RVNGGLLIQD RDLGMVDASQ
410 420 430 440 450
LRVVTERQPS EQELRDALFC WKVAKFVKSN AIVYARDNMT IGIGAGQMSR
460 470 480 490 500
VYSAKIAGIK AGDEGLEVKG SAMASDAFFP FRDGIDAAAA VGITCVIQPG
510 520
GSIRDDEVIA AANEHGIAMI FTDMRHFRH
Length:529
Mass (Da):57,468
Last modified:September 1, 2009 - v1
Checksum:i0081B39C173493EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001657 Genomic DNA Translation: ACT11285.1

Genome annotation databases

EnsemblBacteriaiACT11285; ACT11285; PC1_0225
KEGGipct:PC1_0225

Similar proteinsi

Entry informationi

Entry nameiPUR9_PECCP
AccessioniPrimary (citable) accession number: C6DHT5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: March 28, 2018
This is version 56 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