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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Staphylococcus aureus (strain MW2)
Status
Reviewed-Annotation score: Annotation score: 3 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

BioCyciSAUR196620:GJ9Z-980-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:MW0956
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000418 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Bifunctional purine biosynthesis protein PurHPRO_0000192127Add
BLAST

Proteomic databases

PRIDEiQ8NX88.

Interactioni

Protein-protein interaction databases

STRINGi196620.MW0956.

Structurei

3D structure databases

ProteinModelPortaliQ8NX88.
SMRiQ8NX88. Positions 1-492.
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.

Q8NX88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKAILSVSN KTGIVEFAKA LTQLNYELYS TGGTKRILDE ANVPVRSVSD
60 70 80 90 100
LTHFPEIMDG RVKTLHPAVH GGILADRNKP QHLNELSEQH IDLIDMVVVN
110 120 130 140 150
LYPFQQTVAN PDVTMDEAIE NIDIGGPTML RAAAKNYKHV TTIVHPADYQ
160 170 180 190 200
EVLTRLRNDS LDESYRQSLM IKVFEHTAEY DEAIVRFFKG DKETLRYGEN
210 220 230 240 250
PQQSAYFVRT SNAKHTIAGA KQLHGKQLSY NNIKDADATL ALVKKFDTPA
260 270 280 290 300
TVAVKHMNPC GVGIGDTIEQ AFQHAYEADS QSIFGGIVAL NRAVTPELAE
310 320 330 340 350
QLHSIFLEVI IAPKFTDEAL DILKQKKNVR LLEIDMTIDS NEEEFVSVSG
360 370 380 390 400
GYLVQDKDNY VVPKEEMKVV TEVAPTDEQW EAMLLGWKVV PSVKSNAIIL
410 420 430 440 450
SNNKQTVGIG AGQMNRVGAA KIALERAIEI NDHVALVSDG FFPMGDTVEL
460 470 480 490
AAQHGIKAII QPGGSIKDQD SIDMANKHGI AMVVTGTRHF KH
Length:492
Mass (Da):54,348
Last modified:December 21, 2004 - v2
Checksum:i39C1B60098E53467
GO

Sequence cautioni

The sequence BAB94821.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB94821.1. Different initiation.
RefSeqiNP_645773.1. NC_003923.1.
WP_001790200.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB94821; BAB94821; BAB94821.
KEGGisam:MW0956.
PATRICi19568486. VBIStaAur44266_1002.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB94821.1. Different initiation.
RefSeqiNP_645773.1. NC_003923.1.
WP_001790200.1. NC_003923.1.

3D structure databases

ProteinModelPortaliQ8NX88.
SMRiQ8NX88. Positions 1-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196620.MW0956.

Proteomic databases

PRIDEiQ8NX88.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB94821; BAB94821; BAB94821.
KEGGisam:MW0956.
PATRICi19568486. VBIStaAur44266_1002.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciSAUR196620:GJ9Z-980-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MW2.

Entry informationi

Entry nameiPUR9_STAAW
AccessioniPrimary (citable) accession number: Q8NX88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: December 21, 2004
Last modified: April 29, 2015
This is version 79 of the entry and version 2 of the sequence. [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

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.