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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Streptococcus pneumoniae serotype 19F (strain G54)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciSPNE512566:GCA3-56-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:SPG_0056
OrganismiStreptococcus pneumoniae serotype 19F (strain G54)
Taxonomic identifieri512566 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000008334 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Bifunctional purine biosynthesis protein PurHPRO_1000096100Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi512566.SPG_0056.

Structurei

3D structure databases

ProteinModelPortaliB5E5J9.
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.
HOGENOMiHOG000230372.
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.

B5E5J9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKRVLISVS DKAGIVEFAQ ELKKLGWEII STGGTKVALD NAGVDTIAID
60 70 80 90 100
DMTGFPEMMD GRVKTLHPNI HGGLLARRDL DSHLEAAKDN KIELIDLVVV
110 120 130 140 150
NLYPFKETIL KPDVTYADAV ENIDIGGPSM LRSAAKNHAS VTVVVDPADY
160 170 180 190 200
AVVLDELSAN GETTYETRQR LAAKVFRHTA AYDALIAEYF TAQVGESKPE
210 220 230 240 250
KLTLTYDLKQ AMRYGENPQQ DADFYQKALP TDYSIASAKQ LNGKELSFNN
260 270 280 290 300
IRDADAAIRI IRDFKDRPTV VALKHMNPCG IGQADNIETA WDYAYESDPV
310 320 330 340 350
SIFGGIVVLN REVDAATAEK MHGVFLEIII APSYTDEALA ILINKKKNLR
360 370 380 390 400
ILALPFNAQE ASEVEAEYTG VVGGLLVQNQ DVVKESPADW QVVTKRQPTE
410 420 430 440 450
TEATALEFAW KAIKYVKSNG IIVTNDHMTL GVGPGQTNRV ASVRLAIDQA
460 470 480 490 500
KDRLNGAVLA SDAFFPFADN VEEIAKAGIK AIIQPGGSVR DQESIEAADK
510
YGLTMVFTGV RHFRH
Length:515
Mass (Da):56,397
Last modified:October 14, 2008 - v1
Checksum:iE46354F9CEAC886C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001015 Genomic DNA. Translation: ACF55031.1.
RefSeqiWP_000167074.1. NC_011072.1.
YP_002036771.1. NC_011072.1.

Genome annotation databases

EnsemblBacteriaiACF55031; ACF55031; SPG_0056.
KEGGispx:SPG_0056.
PATRICi19685597. VBIStrPne77426_0053.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001015 Genomic DNA. Translation: ACF55031.1.
RefSeqiWP_000167074.1. NC_011072.1.
YP_002036771.1. NC_011072.1.

3D structure databases

ProteinModelPortaliB5E5J9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi512566.SPG_0056.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF55031; ACF55031; SPG_0056.
KEGGispx:SPG_0056.
PATRICi19685597. VBIStrPne77426_0053.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciSPNE512566:GCA3-56-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: G54.
  2. "Pneumococcal beta glucoside metabolism investigated by whole genome comparison."
    Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M., Tettelin H., Oggioni M.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: G54.

Entry informationi

Entry nameiPUR9_STRP4
AccessioniPrimary (citable) accession number: B5E5J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: May 27, 2015
This is version 49 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

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.