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B5ZV31 (PUR9_RHILW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:Rleg2_3915
OrganismRhizobium leguminosarum bv. trifolii (strain WSM2304) [Complete proteome] [HAMAP]
Taxonomic identifier395492 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length538 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 – 538538Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096087

Sequences

Sequence LengthMass (Da)Tools
B5ZV31 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 00D02314897764F2

FASTA53857,027
        10         20         30         40         50         60 
MAVISKKIPA PDKVEIKTAL LSVFDKTGIV ELAQALSEQG VRLLSTGGTY KAIAAAGLAV 

        70         80         90        100        110        120 
TDVSEITGFP EIMDGRVKTL HPTVHGGLLA IRDDSEHQEA MKTHGIEAID LAVINLYPFE 

       130        140        150        160        170        180 
DVRAAGGDYP TTVENIDIGG PAMIRASAKN HAYVTILTDP NDYAEFTEQL SADGGKTAYA 

       190        200        210        220        230        240 
FRQRMAAKAY ARTAAYDAVI SNWFAEALSI DTPRHRVIGG ALKEEMRYGE NPHQKAAFYV 

       250        260        270        280        290        300 
TGEKRPGVST AALLQGKQLS YNNINDTDAA YELVAEFLPE KEPACAIIKH ANPCGVATGS 

       310        320        330        340        350        360 
SLVEAYRRAL ACDSVSAFGG IIALNRTLDA ETAEEIVKLF TEVIIAPDVT EEAKAIIARK 

       370        380        390        400        410        420 
PNLRLLSAGG LPDPRAAGLT AKTVSGGLLV QSRDNGMVED LELKVVTKRA PTAQELDDMK 

       430        440        450        460        470        480 
FAFKIGKHVK SNAVVYAKDG QTAGIGAGQM SRVDSARIAA LKAEEAAKAL GLAVPMTHGS 

       490        500        510        520        530 
AVASEAFLPF ADGLLSMIAA GATAVIQPGG SMRDQEVIDA ADEHGIAMVF TGMRHFRH 

« Hide

References

[1]"Complete sequence of chromosome of Rhizobium leguminosarum bv. trifolii WSM2304."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Yates R. expand/collapse author list , Ardley J., Tiwari R.P., O'Hara G., Howieson J., Brau L., Reeve W.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM2304.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001191 Genomic DNA. Translation: ACI57177.1.
RefSeqYP_002283403.1. NC_011369.1.

3D structure databases

ProteinModelPortalB5ZV31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395492.Rleg2_3915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI57177; ACI57177; Rleg2_3915.
GeneID6982679.
KEGGrlt:Rleg2_3915.
PATRIC23132116. VBIRhiLeg95088_5857.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycRLEG395492:GJB3-3971-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_RHILW
AccessionPrimary (citable) accession number: B5ZV31
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: May 14, 2014
This is version 40 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