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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Pseudomonas aeruginosa (strain LESB58)
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

BioCyciPAER557722:GHJW-5326-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:PLES_52391
OrganismiPseudomonas aeruginosa (strain LESB58)
Taxonomic identifieri557722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000001527 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535Bifunctional purine biosynthesis protein PurHPRO_1000192979Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi557722.PLES_52391.

Structurei

3D structure databases

ProteinModelPortaliB7V1R6.
SMRiB7V1R6. Positions 7-535.
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.

B7V1R6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDQTTRLPI RRALISVSDK TGVVDFAREL VALGVEILST GGTYKLLRDN
60 70 80 90 100
GISAVEVADY TGFPEMMDGR VKTLHPKVHG GILGRRDLDG AVMEQHGIKP
110 120 130 140 150
IDLVAVNLYP FEATVARPDC DLPTAIENID IGGPTMVRSA AKNHKDVAIV
160 170 180 190 200
VNAGDYAAVI ESLKAGGLTY AQRFDLALKA FEHTSAYDGM IANYLGTIDQ
210 220 230 240 250
TRDTLGTADR GAFPRTFNSQ FVKAQEMRYG ENPHQSAAFY VEAKKGEASV
260 270 280 290 300
STAIQLQGKE LSFNNVADTD AALECVKSFL KPACVIVKHA NPCGVAVVPE
310 320 330 340 350
DEGGIRKAYD LAYATDSESA FGGIIAFNRE LDGETAKAIV ERQFVEVIIA
360 370 380 390 400
PKISAAAREV VAAKANVRLL ECGEWPAERA PGWDFKRVNG GLLVQSRDIG
410 420 430 440 450
MIKAEDLKIV TRRAPTEQEI HDLIFAWKVA KFVKSNAIVY ARNRQTVGVG
460 470 480 490 500
AGQMSRVNSA RIAAIKAEHA GLEVKGAVMA SDAFFPFRDG IDNAAKAGIT
510 520 530
AVIQPGGSMR DNEVIAAADE ADIAMVFTGM RHFRH
Length:535
Mass (Da):57,666
Last modified:February 10, 2009 - v1
Checksum:i38B912B9570E23BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM209186 Genomic DNA. Translation: CAW29993.1.
RefSeqiWP_003105151.1. NC_011770.1.
YP_002442817.1. NC_011770.1.

Genome annotation databases

EnsemblBacteriaiCAW29993; CAW29993; PLES_52391.
KEGGipag:PLES_52391.
PATRICi19820378. VBIPseAer113719_5385.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM209186 Genomic DNA. Translation: CAW29993.1.
RefSeqiWP_003105151.1. NC_011770.1.
YP_002442817.1. NC_011770.1.

3D structure databases

ProteinModelPortaliB7V1R6.
SMRiB7V1R6. Positions 7-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi557722.PLES_52391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAW29993; CAW29993; PLES_52391.
KEGGipag:PLES_52391.
PATRICi19820378. VBIPseAer113719_5385.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciPAER557722:GHJW-5326-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. "Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa."
    Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.
    Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LESB58.

Entry informationi

Entry nameiPUR9_PSEA8
AccessioniPrimary (citable) accession number: B7V1R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 27, 2015
This is version 46 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.