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
Staphylococcus carnosus (strain TM300)
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.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciSCAR396513:GJ9G-710-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:Sca_0695
OrganismiStaphylococcus carnosus (strain TM300)
Taxonomic identifieri396513 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000444 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Bifunctional purine biosynthesis protein PurHPRO_1000122971Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi396513.Sca_0695.

Structurei

3D structure databases

ProteinModelPortaliB9DQ42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

B9DQ42-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVILSVSD KSGIVDFAKS LVGLDYELYS TGGTKRALDE AGVPVKSVSD
60 70 80 90 100
LTQFDEIMDG RVKTLHPAVH GGILADRDKP EHLQQLKDKG IDLIDIVVVN
110 120 130 140 150
LYPFKETVAN PDVTEMDAIE NIDIGGPTML RAAAKNFKHV TTIVDPSDYD
160 170 180 190 200
EVIEHIKNDS LDETFRKSLM IKVFEHTNDY DNAIVNFFKE NKEPLRYGEN
210 220 230 240 250
PQQDAYFVRT SDAPNTIAGA KQLHGKQLSF NNIKDADATL ALAKKFEEPA
260 270 280 290 300
AVAVKHMNPC GVGVGSSIEE AFQNAYDADS QSIFGGIVAV NRPVTKELAE
310 320 330 340 350
KLHSIFLEVV IAPSFTEEAL EVLTKKKNIR LLEVEMTVDH DEKEYVSVSG
360 370 380 390 400
GYLVQDKDTK TISRDDMKVV TKAEPTEEQW KAMELGWKVV PSVKSNAIIL
410 420 430 440 450
SNDHQTVGIG AGQMNRVGSA EIAIERAIEI NDNVALVSDG FFPMDDTVEL
460 470 480 490
AAKAGIKAII QPGGSIKDQD SIDMADKHGI AMVMTGVRHF KH
Length:492
Mass (Da):54,037
Last modified:March 24, 2009 - v1
Checksum:iE6713639B6CE6C0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM295250 Genomic DNA. Translation: CAL27606.1.
RefSeqiYP_002633791.1. NC_012121.1.

Genome annotation databases

KEGGisca:Sca_0695.
PATRICi19602166. VBIStaCar105558_0698.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM295250 Genomic DNA. Translation: CAL27606.1.
RefSeqiYP_002633791.1. NC_012121.1.

3D structure databases

ProteinModelPortaliB9DQ42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi396513.Sca_0695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGisca:Sca_0695.
PATRICi19602166. VBIStaCar105558_0698.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciSCAR396513:GJ9G-710-MONOMER.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome analysis of the meat starter culture bacterium Staphylococcus carnosus TM300."
    Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C., Goetz F.
    Appl. Environ. Microbiol. 75:811-822(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TM300.

Entry informationi

Entry nameiPUR9_STACT
AccessioniPrimary (citable) accession number: B9DQ42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: April 1, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.