Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2K2T6 (PUR9_RHIEC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:RHE_CH04107
OrganismRhizobium etli (strain CFN 42 / ATCC 51251) [Complete proteome] [HAMAP]
Taxonomic identifier347834 [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_1000018947

Sequences

Sequence LengthMass (Da)Tools
Q2K2T6 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 2FA8DBB6E81B62DD

FASTA53857,150
        10         20         30         40         50         60 
MAVISKKIPA PDKVEIKTAL LSVFDKTGIV ELAQALSERG VRLLSTGGTY KAIAAAGLAV 

        70         80         90        100        110        120 
TDVSDITGFP EIMDGRVKTL HPTVHGGLLA IRDDNEHQEA MKKHGIEGID LAVINLYPFE 

       130        140        150        160        170        180 
EVRAAGGDYP TTVENIDIGG PAMIRASAKN HAYVTILTDP NDYAEFKEQL SADAGKTAYA 

       190        200        210        220        230        240 
FRQRMAAKAY ARTAAYDAAI SNWFAEALSI DTPRHRVIGG VLKEEMRYGE NPHQRAAFYV 

       250        260        270        280        290        300 
TGEKRPGVST AVLLQGKQLS YNNINDTDAA YELVAEFLPE RAPACAIIKH ANPCGVATGS 

       310        320        330        340        350        360 
SLIEAYQRAL ACDSVSAFGG IIALNQILDA ETAEEIVKLF TEVIIAPDVT EEAKAIVARK 

       370        380        390        400        410        420 
PNLRLLSAGG LPDPRVAGLT AKTVSGGLLV QSRDNGMVED LELKVVTRRA PTGQELEDMK 

       430        440        450        460        470        480 
FAFKVGKHVK SNAVVYAKDG QTAGIGAGQM SRVDSARIAA LKAEEAAKAL GLAVPMTKGS 

       490        500        510        520        530 
AVASEAFLPF ADGLLSMIAA GATAVIQPGG SMRDQEVIDA ANEHGIAMVF TGMRHFRH 

« Hide

References

[1]"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons."
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFN 42 / ATCC 51251.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000133 Genomic DNA. Translation: ABC92850.1.
RefSeqYP_471577.1. NC_007761.1.

3D structure databases

ProteinModelPortalQ2K2T6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347834.RHE_CH04107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC92850; ABC92850; RHE_CH04107.
GeneID3892030.
KEGGret:RHE_CH04107.
PATRIC23089968. VBIRhiEtl108884_4616.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMACGVATGP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycRETL347834:GJJ0-4125-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_RHIEC
AccessionPrimary (citable) accession number: Q2K2T6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 58 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