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
Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
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

BioCyciSCEL448385:G1GJQ-3241-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:sce3150
OrganismiSorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56))
Taxonomic identifieri448385 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesSorangiineaePolyangiaceaeSorangium
Proteomesi
  • UP000002139 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000764961 – 522Bifunctional purine biosynthesis protein PurHAdd BLAST522

Interactioni

Protein-protein interaction databases

STRINGi448385.sce3150

Structurei

3D structure databases

ProteinModelPortaliA9GIT1
SMRiA9GIT1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 143MGS-likePROSITE-ProRule annotationAdd BLAST143

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.

A9GIT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRRALISVS DKTGLLPLAR RLAEKGVEIL STGGTQRALA DAGVPVIGVE
60 70 80 90 100
AYTGSPEVMD GRVKTLHPRV HGGILMRGAI DDEDLARLGG APIDLVVCNL
110 120 130 140 150
YPFEATVRKP GVTHPEIIEN IDIGGPSMVR SAAKNHARVA VVVDPADYDA
160 170 180 190 200
VLAEIDRQGE VSSATRRRLA TKAFAHTAAY DGMVSGYLSS LPEEGEPSAA
210 220 230 240 250
EREAYPRFLT LALERAYPLR YGENPHQSGA FYRERGAAAG SLALAESLGA
260 270 280 290 300
GGKELSFNNL VDVDAAFEAV REFTQPAAVV VKHTNPCGVA TGDSLAAAYR
310 320 330 340 350
TARDADAVSA FGGIVALNRE VDRAAAEVLV ETFLECVVAP AYTPDALEVL
360 370 380 390 400
RTKKNLRLLA TGALLPADHR ELTFKRVGGG LVVQERDASA AGEVRGGRVV
410 420 430 440 450
AKRAPTEEEI EALDLGWRVC KHVKSNAIVL AIPGRTVGIG AGQMSRVESV
460 470 480 490 500
RIACSKAGER ARGSVLASDA FFPFPDNVVL AAEHGITAVA QPGGSVKDAE
510 520
VIAAADAAGI AMVFTGARHF RH
Length:522
Mass (Da):54,941
Last modified:February 5, 2008 - v1
Checksum:iE4733BE708CFE02F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM746676 Genomic DNA Translation: CAN93309.1
RefSeqiWP_012235781.1, NC_010162.1

Genome annotation databases

EnsemblBacteriaiCAN93309; CAN93309; sce3150
KEGGiscl:sce3150

Similar proteinsi

Entry informationi

Entry nameiPUR9_SORC5
AccessioniPrimary (citable) accession number: A9GIT1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: March 28, 2018
This is version 67 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health