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
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Unreviewed-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 annotationSAAS annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotationSAAS 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 annotationSAAS 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 annotationSAAS 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 functionHydrolaseUniRule annotationSAAS annotationImported, Multifunctional enzymeUniRule annotationSAAS annotation, TransferaseUniRule annotationSAAS annotationImported
Biological processPurine biosynthesisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciTTHE300852:G1GKC-940-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
InosinicaseUniRule annotation
IMP synthaseUniRule annotation
Gene namesi
Name:purHUniRule annotation
Ordered Locus Names:TTHA0930Imported
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)Imported
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA0930

Structurei

3D structure databases

ProteinModelPortaliQ5SJS8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 126MGSInterPro annotationAdd BLAST112

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105DC1 Bacteria
COG0138 LUCA
HOGENOMiHOG000230373
KOiK00602
OMAiDLLFAWK
PhylomeDBiQ5SJS8

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

Sequencei

Sequence statusi: Complete.

Q5SJS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSMWALLSV ADKRGIVDFA RGLAELGFRL LATGGTYRAL REAGLPVTYI
60 70 80 90 100
SDFTGFPEIL EGRVKTLHPK VHAALLARPD QEEELKALGL ERIGVLAVNL
110 120 130 140 150
YPFRETVARG ASFAEALEQI DIGGPAMLRA AAKNHQAVLP VCDPEDYPRV
160 170 180 190 200
LEALKAGPSP DFRQKLARKA FAHTALYDAA IAEWLSGEKF PEEKLLALRR
210 220 230 240 250
EASLRYGENP HQEAALYRVV GERGPLLEAQ VLQGKAMSFN NYLDAEAAWN
260 270 280 290 300
LVSEFAEPAC VAVKHQNPCG VALGETPLEA YRKAYEADPV SIFGGIVAFN
310 320 330 340 350
RPLDGPTAEA LAEVFLEVVL APSFSPEARA VLARKKNLRL LQVPFPAQGP
360 370 380 390 400
YLDLRRLRGG VLLQDADTED PAEPKVVTER APTPEEWPDL RFAWKVVKHV
410 420 430 440 450
RSNAIVVAKG GMTLGIGVGQ TNRLAAARHA LEAAGERAKG AVLASDAFFP
460 470 480 490
FDDVVRLAAS YGIAAIIQPG GSVRDQDSIR AAEEAGIAMV FTGVRHFRH
Length:499
Mass (Da):54,200
Last modified:December 21, 2004 - v1
Checksum:iE6E08A406B79432D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA Translation: BAD70753.1
RefSeqiWP_011173006.1, NC_006461.1
YP_144196.1, NC_006461.1

Genome annotation databases

EnsemblBacteriaiBAD70753; BAD70753; BAD70753
GeneIDi3169136
KEGGittj:TTHA0930
PATRICifig|300852.9.peg.913

Similar proteinsi

Entry informationi

Entry nameiQ5SJS8_THET8
AccessioniPrimary (citable) accession number: Q5SJS8
Entry historyiIntegrated into UniProtKB/TrEMBL: December 21, 2004
Last sequence update: December 21, 2004
Last modified: May 23, 2018
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

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