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
Shewanella frigidimarina (strain NCIMB 400)
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

BioCyciSFRI318167:G1G77-511-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:Sfri_0493
OrganismiShewanella frigidimarina (strain NCIMB 400)
Taxonomic identifieri318167 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000000684 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000189521 – 529Bifunctional purine biosynthesis protein PurHAdd BLAST529

Interactioni

Protein-protein interaction databases

STRINGi318167.Sfri_0493

Structurei

3D structure databases

ProteinModelPortaliQ088G0
SMRiQ088G0
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
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.

Q088G0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNVRPIRRA LLSVSDKTGI LEFAQALHAQ GVELLSTGGT AKLLADNNIP
60 70 80 90 100
VMEVSDYTGH PEIMDGRVKT LHPKIHGGIL ARRGIDEIVM EQNAIKPIDL
110 120 130 140 150
VTVNLYPFAE TVAKPGCTLA DAVENIDIGG PTMVRSTAKN HKDTTIVVNA
160 170 180 190 200
KDYGRVIAEM QANNGSTTLE TRFDLAIAAF EHTAAYDGMI ANYFGTMVPA
210 220 230 240 250
HSNDECHDDS TFPRTFNSQF VKKQDLRYGE NSHQKAAFYV DTQIDEASVA
260 270 280 290 300
SAIQLQGKAL SYNNIADTDS ALECVKEFEG PACVIVKHAN PCGVALGANL
310 320 330 340 350
LEAYDRAFKT DPTSAFGGII AFNQELDAQT AQAIVDRQFV EVIIAPKVSQ
360 370 380 390 400
AARDIIAAKA NVRLLECGEW NTKTTTLDYK RVNGGLLIQD RDQGMVNLED
410 420 430 440 450
VKVVSKRQPT AEQLKDLMFC WKVAKFVKSN AIVYAKDGMT IGVGAGQMSR
460 470 480 490 500
VYSAKIAGIK AADEGLVVEN SVMASDAFFP FRDGIDAAAA AGISCIIQPG
510 520
GSIRDEEIIA AADEHGMAMV FTGMRHFRH
Length:529
Mass (Da):57,247
Last modified:October 31, 2006 - v1
Checksum:i7A8C35EDB35BF4E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000447 Genomic DNA Translation: ABI70355.1
RefSeqiWP_011635982.1, NC_008345.1

Genome annotation databases

EnsemblBacteriaiABI70355; ABI70355; Sfri_0493
KEGGisfr:Sfri_0493

Similar proteinsi

Entry informationi

Entry nameiPUR9_SHEFN
AccessioniPrimary (citable) accession number: Q088G0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 31, 2006
Last modified: March 28, 2018
This is version 72 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health