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A4T025 (PUR9_POLSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:Pnuc_1877
OrganismPolynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1) [Complete proteome] [HAMAP]
Taxonomic identifier312153 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaePolynucleobacter

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076488

Sequences

Sequence LengthMass (Da)Tools
A4T025 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 0C816811F14922EB

FASTA52656,551
        10         20         30         40         50         60 
MIRTALLSVS DKNGIVPFAK SLHEQGIKLI STGGTAKLLA ENNLPVVEVS SLTKFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPMV HGGLLARRDF PEHMAALEEH GIDTIDMLVI NLYPFNETVA KENCSFEDAV 

       130        140        150        160        170        180 
ENIDIGGPAM LRAAAKNHQD VTVLISPEDY APVLAEMKAN QNVVSYKTNL ALAKKVFAHT 

       190        200        210        220        230        240 
AQYDGSIANY LSALGDDLDH KARSAYPETL HLAFEKVQEM RYGENPHQSA AFYKDIYPVN 

       250        260        270        280        290        300 
GALANYKQLQ GKELSYNNIA DADSAWECVK SFAGNSGGAA ACVIIKHANP CGVAVGASAL 

       310        320        330        340        350        360 
EAYQKAFKTD PSSAFGGIIA FNIPCDGAAA QEISKQFVEV LIAPSFTDEA KAIFAAKQNV 

       370        380        390        400        410        420 
RLLEIPLGNA FNTFDFKRVG GGLLVQSPDA KNVLQNEMRV VSQRQPTPSE MNDMMFAWRV 

       430        440        450        460        470        480 
AKFVKSNAIV YCSNGMTLGI GAGQMSRVDS ARMASIKAEN AGLSLKGSAV ASDAFFPFRD 

       490        500        510        520 
GLDVVVNGGA SCAIQPGGSM RDDEIIAAAN EHGIAMIFTG TRHFRH 

« Hide

References

[1]"Complete genome sequence of Polynucleobacter necessarius subsp. asymbioticus type strain (QLW-P1DMWA-1(T))."
Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.
Stand. Genomic Sci. 6:74-83(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 18221 / CIP 109841 / QLW-P1DMWA-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000655 Genomic DNA. Translation: ABP35089.1.
RefSeqYP_001156653.1. NC_009379.1.

3D structure databases

ProteinModelPortalA4T025.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312153.Pnuc_1877.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP35089; ABP35089; Pnuc_1877.
GeneID5053927.
KEGGpnu:Pnuc_1877.
PATRIC22968277. VBIPolNec12025_1943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycPNEC312153:GH50-1918-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_POLSQ
AccessionPrimary (citable) accession number: A4T025
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: February 19, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways