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P57828 (PUR9_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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:PM0222
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length533 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 – 533533Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192111

Sequences

Sequence LengthMass (Da)Tools
P57828 [UniParc].

Last modified April 27, 2001. Version 1.
Checksum: 2D2C4EB4CC0B63A4

FASTA53358,084
        10         20         30         40         50         60 
MQPNRPIRQA LLSVSDKTGI VEFAQALVQR GVKLLSTGGT AKLLADHGLA VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRGTDDEVM SQQGIEGIDM VVVNLYPFAA TVAKPNCSLE 

       130        140        150        160        170        180 
EAVENIDIGG PTMVRSAAKN HQDVAIVVNN SDFNAILAEM DQHQNSLTLE TRFDLAIKAF 

       190        200        210        220        230        240 
EHTAQYDAMI ANYFGQLVKP YFVAEEEDAE AKCGQFPRTL NLNFIRKQTM RYGENGHQKA 

       250        260        270        280        290        300 
AFYVEQDVKE ASVSTAKQLQ GKALSYNNIA DTDAALECVK SFDEPACVIV KHANPCGVAL 

       310        320        330        340        350        360 
GADILAAYNR AYQTDPTSAF GGIIAFNREL DAKTAQTIID RQFVEVIIAP TVAEEAKALL 

       370        380        390        400        410        420 
KAKKNVRVLE CGEWSGTQQR LDVKRVNGGL LVQEADLGMV DLADLKVVSK RQPTEQELKD 

       430        440        450        460        470        480 
LLFCWKVAKF VKSNAIVYAK DNQTIGIGAG QMSRVYSAKI AGIKAQDEGL DVAGCVMASD 

       490        500        510        520        530 
AFFPFRDGID AAAKVGIQCV IHPGGSMRDQ EVIDAADEHN MVMVLTGMRH FRH 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK02306.1.
RefSeqNP_245159.1. NC_002663.1.

3D structure databases

ProteinModelPortalP57828.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM0222.

Proteomic databases

PRIDEP57828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK02306; AAK02306; PM0222.
GeneID1243569.
KEGGpmu:PM0222.
PATRIC22869596. VBIPasMul88067_0230.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMALKSTLRY.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-226-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_PASMU
AccessionPrimary (citable) accession number: P57828
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: May 14, 2014
This is version 83 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