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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-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.
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

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).
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.
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, Transferase
Biological processPurine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:purH
Ordered Locus Names:SH1884
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000543 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000189641 – 492Bifunctional purine biosynthesis protein PurHAdd BLAST492

Interactioni

Protein-protein interaction databases

STRINGi279808.SH1884.

Structurei

3D structure databases

ProteinModelPortaliQ4L582.
SMRiQ4L582.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.

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.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
IPR036914. MGS-like_dom_sf.
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.

Q4L582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKAILSVSN KSGIVEFAKS LIKLDYELYS TGGTKGALED ASVPVKSVSE
60 70 80 90 100
LTQFPEIMDG RVKTLHPAVH GGILADRDKP EHLEQLSEQH IDLIDMVVVN
110 120 130 140 150
LYPFQKTVAK PDVTEAEAIE NIDIGGPTML RAAAKNFKHV TTIVHPADYN
160 170 180 190 200
EVIERIKEDR LDEDFRKELM IKVFAHTNEY DHAIVSFFKG DSEQLRYGEN
210 220 230 240 250
PQQSARFVRT SNSKHTIAGA KQLHGKALSF NNIKDADSAL SLVKKFKESA
260 270 280 290 300
AVAVKHMNPC GVGIGDNIET AFKHAYDADN QSIFGGIIAL NRTVTSDLAE
310 320 330 340 350
TLHAIFLEVV IAPRFTDEAL DILTKKKNIR LLEIDMTIDN REEEFVSVSG
360 370 380 390 400
GYLVQDKDNF EVAKEDMKVV TDKAPTDDQW DAMLLGWKVI PSVKSNAVIL
410 420 430 440 450
SNTKQTVGIG AGQMNRVGSA KIALERAIEI NDNVALVSDG FFPMDDTVEL
460 470 480 490
AAQHGIKAII QPGGSIKDQD SIDMANKYGI AMVTTGMRHF KH
Length:492
Mass (Da):54,216
Last modified:August 2, 2005 - v1
Checksum:i03C0512577303EC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05193.1.
RefSeqiWP_011276157.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05193; BAE05193; SH1884.
GeneIDi24245865.
KEGGisha:SH1884.

Similar proteinsi

Entry informationi

Entry nameiPUR9_STAHJ
AccessioniPrimary (citable) accession number: Q4L582
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 2, 2005
Last modified: November 22, 2017
This is version 90 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, Multifunctional enzyme

Documents

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