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Q2RN46 (PUR9_RHORT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:Rru_A3655
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Reference proteome] [HAMAP]
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057908

Sequences

Sequence LengthMass (Da)Tools
Q2RN46 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: FA0A3D508625142B

FASTA52655,399
        10         20         30         40         50         60 
MLHSLPIRRA LISVSDKGGL VPFARFLADH DIEILSTGGS AKALADAGIP VTEVADFTGF 

        70         80         90        100        110        120 
PEMLDGRVKT LHPKIHGGIL GIRDNPEHQR AMAAHEILPI DLVVVNLYPF EATVAKGAAF 

       130        140        150        160        170        180 
EDCVENIDIG GPALIRAAAK NHEAVTVVVD PEDYQPVMDA MTAEGGATTL ELRRKLASAA 

       190        200        210        220        230        240 
FARCGAYDGA ISRWFQGQVG DETPRHIVFA GRLRQTLRYG ENPHQKAAFY GHGIARPGVA 

       250        260        270        280        290        300 
SAEQLQGKEL SYNNINDTDA AFDLVCEFAE PAVAIIKHAN PCGVAQGASV VEAYKAALAC 

       310        320        330        340        350        360 
DPVSAFGGIV ALNRPIDRDS AVEITKIFTE VVIAPDADAE ARAIFAAKKN LRLLLTGVVA 

       370        380        390        400        410        420 
DTTAPGLTVR SVAGGMLVQD RDAADLLSAD LKVVSKRTPT ERELADMLIA FKVCKHVKSN 

       430        440        450        460        470        480 
AIVYVKDGAT VGIGAGQMSR VDSARIASWK ADEAAEAAGL AQSPTQGSVV ASDAFFPFAD 

       490        500        510        520 
GLLAAAKAGA TAVIQPGGSM RDDEVIKAAD EAGLAMVFTG LRHFRH 

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000230 Genomic DNA. Translation: ABC24449.1.
RefSeqYP_428736.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RN46.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269796.Rru_A3655.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC24449; ABC24449; Rru_A3655.
GeneID3837111.
KEGGrru:Rru_A3655.
PATRIC23331120. VBIRhoRub82919_3777.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMACGVATGP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycRRUB269796:GCN1-3719-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_RHORT
AccessionPrimary (citable) accession number: Q2RN46
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 61 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