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A6UED3 (PUR9_SINMW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:Smed_3189
OrganismSinorhizobium medicae (strain WSM419) (Ensifer medicae) [Complete proteome] [HAMAP]
Taxonomic identifier366394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length536 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 – 536536Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018959

Sequences

Sequence LengthMass (Da)Tools
A6UED3 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: CF971062CCDAC359

FASTA53656,481
        10         20         30         40         50         60 
MAVASKKIPA PDEVRIKTAL LSVSDKSGIV ELARHLNDRG VRLVSTGGTH KALADAGLPV 

        70         80         90        100        110        120 
SDVSELTGFP EIMDGRVKTL HPGVHGGLLA IRDDAEHAGA MSAHGITAID LAVINLYPFE 

       130        140        150        160        170        180 
EVRAKGGDYP TTVENIDIGG PAMIRASAKN HAYVTVVTDP ADYPLLLEEI AGGTTRYAFR 

       190        200        210        220        230        240 
QKMAAKAYAR TAAYDAAISN WFAEVLDTPM PRHRVIGGVL KEEMRYGENP HQKAGFYVTG 

       250        260        270        280        290        300 
DKRPGVATAA LLQGKQLSYN NINDTDAAFE LVAEFLPEKA PACAIIKHAN PCGVATAPSL 

       310        320        330        340        350        360 
AEAYRRALAC DSTSAFGGII ALNQELDAAT AEEIVKLFTE VIIAPSVSDE AKAIIARKPN 

       370        380        390        400        410        420 
LRLLATGGLP DPRTPGLTAK TVAGGLLVQT RDDGMIEDIE LKVVTKRTPT AQELEDMKFA 

       430        440        450        460        470        480 
FKVAKHVKSN AVVYAKGGQT AGIGAGQMSR VDSARIAAIK AEEAAKALGL AEPLTRGSAV 

       490        500        510        520        530 
ASEAFLPFAD GLLSAIAAGA TAVIQPGGSM RDEEVIAAAD EHNVAMVFTG MRHFRH 

« Hide

References

[1]"Complete sequence of Sinorhizobium medicae WSM419 chromosome."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM419.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000738 Genomic DNA. Translation: ABR62013.1.
RefSeqYP_001328848.1. NC_009636.1.

3D structure databases

ProteinModelPortalA6UED3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING366394.Smed_3189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR62013; ABR62013; Smed_3189.
GeneID5324068.
KEGGsmd:Smed_3189.
PATRIC23625617. VBISinMed134228_6426.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSMED366394:GJAL-3241-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_SINMW
AccessionPrimary (citable) accession number: A6UED3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 46 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