SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P67544

- PUR9_STAAN

UniProt

P67544 - PUR9_STAAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional purine biosynthesis protein PurH

Gene
purH, SA0925
Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-977-MONOMER.
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:SA0925
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Bifunctional purine biosynthesis protein PurHUniRule annotationPRO_0000192124Add
BLAST

Proteomic databases

PRIDEiP67544.

Interactioni

Protein-protein interaction databases

STRINGi158879.SA0925.

Structurei

3D structure databases

ProteinModelPortaliP67544.
SMRiP67544. Positions 1-492.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiRAFKTDP.
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.

P67544-1 [UniParc]FASTAAdd to Basket

« Hide

MKKAILSVSN KTGIVEFAKA LTQLNYELYS TGGTKRILDE ANVPVRSVSD    50
LTHFPEIMDG RVKTLHPAVH GGILADRNKP QHLNELSEQH IDLIDMVVVN 100
LYPFQQTVAN PDVTMDEAIE NIDIGGPTML RAAAKNYKHV TTIVHPADYH 150
EVLTRLRNDS LDESYRQSLM IKVFEHTAEY DEAIVRFFKG DKETLRYGEN 200
PQQSAYFVRT SNAKHTIAGA KQLHGKQLSY NNIKDADATL ALVKKFDTPA 250
AVAVKHMNPC GVGIGDTIEQ AFQHAYEADS QSIFGGIVAL NRAVTPELAE 300
QLHSIFLEVI IAPKFTDEAL DILKQKKNVR LLEIDMTIDS NEEEFVSVSG 350
GYLVQDKDNY VVPKEEMKVV TEVAPTDEQW EAMLLGWKVV PSVKSNAIIL 400
SNNKQTVGIG AGQMNRVGAA KIALERAIEI NDHVALVSDG FFPMGDTVEL 450
AAQHGIKAII QPGGSIKDQD SIDMANKHGI AMVVTGTRHF KH 492
Length:492
Mass (Da):54,327
Last modified:December 21, 2004 - v2
Checksum:iC744D79C547EDDA8
GO

Sequence cautioni

The sequence BAB42170.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42170.1. Different initiation.
PIRiG89876.
RefSeqiNP_374192.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42170; BAB42170; BAB42170.
GeneIDi1123748.
KEGGisau:SA0925.
PATRICi19574038. VBIStaAur116463_0989.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB42170.1 . Different initiation.
PIRi G89876.
RefSeqi NP_374192.1. NC_002745.2.

3D structure databases

ProteinModelPortali P67544.
SMRi P67544. Positions 1-492.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA0925.

Proteomic databases

PRIDEi P67544.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB42170 ; BAB42170 ; BAB42170 .
GeneIDi 1123748.
KEGGi sau:SA0925.
PATRICi 19574038. VBIStaAur116463_0989.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci SAUR158879:GJCB-977-MONOMER.

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiPUR9_STAAN
AccessioniPrimary (citable) accession number: P67544
Secondary accession number(s): Q99V24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: December 21, 2004
Last modified: May 14, 2014
This is version 70 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