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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
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:Rru_A3655
OrganismiRhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Taxonomic identifieri269796 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum
Proteomesi
  • UP000001929 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000579081 – 526Bifunctional purine biosynthesis protein PurHAdd BLAST526

Proteomic databases

PRIDEiQ2RN46

Interactioni

Protein-protein interaction databases

STRINGi269796.Rru_A3655

Structurei

3D structure databases

ProteinModelPortaliQ2RN46
SMRiQ2RN46
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 149MGS-likePROSITE-ProRule annotationAdd BLAST149

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
HOGENOMiHOG000230372
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.

Q2RN46-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHSLPIRRA LISVSDKGGL VPFARFLADH DIEILSTGGS AKALADAGIP
60 70 80 90 100
VTEVADFTGF PEMLDGRVKT LHPKIHGGIL GIRDNPEHQR AMAAHEILPI
110 120 130 140 150
DLVVVNLYPF EATVAKGAAF EDCVENIDIG GPALIRAAAK NHEAVTVVVD
160 170 180 190 200
PEDYQPVMDA MTAEGGATTL ELRRKLASAA FARCGAYDGA ISRWFQGQVG
210 220 230 240 250
DETPRHIVFA GRLRQTLRYG ENPHQKAAFY GHGIARPGVA SAEQLQGKEL
260 270 280 290 300
SYNNINDTDA AFDLVCEFAE PAVAIIKHAN PCGVAQGASV VEAYKAALAC
310 320 330 340 350
DPVSAFGGIV ALNRPIDRDS AVEITKIFTE VVIAPDADAE ARAIFAAKKN
360 370 380 390 400
LRLLLTGVVA DTTAPGLTVR SVAGGMLVQD RDAADLLSAD LKVVSKRTPT
410 420 430 440 450
ERELADMLIA FKVCKHVKSN AIVYVKDGAT VGIGAGQMSR VDSARIASWK
460 470 480 490 500
ADEAAEAAGL AQSPTQGSVV ASDAFFPFAD GLLAAAKAGA TAVIQPGGSM
510 520
RDDEVIKAAD EAGLAMVFTG LRHFRH
Length:526
Mass (Da):55,399
Last modified:January 24, 2006 - v1
Checksum:iFA0A3D508625142B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000230 Genomic DNA Translation: ABC24449.1
RefSeqiWP_011391402.1, NC_007643.1
YP_428736.1, NC_007643.1

Genome annotation databases

EnsemblBacteriaiABC24449; ABC24449; Rru_A3655
GeneIDi3837111
KEGGirru:Rru_A3655
PATRICifig|269796.9.peg.3777

Similar proteinsi

Entry informationi

Entry nameiPUR9_RHORT
AccessioniPrimary (citable) accession number: Q2RN46
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 24, 2006
Last modified: May 23, 2018
This is version 79 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

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