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Q1GKJ2 (PUR9_RUEST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:TM1040_0091
OrganismRuegeria sp. (strain TM1040) (Silicibacter sp.) [Complete proteome] [HAMAP]
Taxonomic identifier292414 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length529 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 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057915

Sequences

Sequence LengthMass (Da)Tools
Q1GKJ2 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 9358E2A8E01EA7CD

FASTA52956,292
        10         20         30         40         50         60 
MTDLHPVRRA LLSVSDKTGL IELGKSLAER GVELLSTGGT AKALRDAGLT VKDVSEVTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPMVHGGLL ALRDNDAHVA AMTDHGIGEI DLLVVNLYPF EAALKRGAAY 

       130        140        150        160        170        180 
DEMIENIDIG GPAMIRAAAK NHAFVNVVVD VEDYGVLLEE LDQNDGQTSF AFRQWLAQNA 

       190        200        210        220        230        240 
YARTAAYDAA VSNWMAGAIG LDAPRRRAFA GQIAQTLRYG ENPHQDAAFY TDGTERVGVA 

       250        260        270        280        290        300 
TAEQLQGKEL SYNNINDTDA AFELVSEFAP EDGPAVAIIK HANPCGVARG ATLLEAYNKA 

       310        320        330        340        350        360 
FDCDRTSAFG GIVALNMPLD AETAEAITQI FTEVVIAPGA SDEAKAIFAA KKNLRLLITE 

       370        380        390        400        410        420 
GLPNPQDAGL TTRQVSGGML VQDKDVGHRA MDDLKVVTEK APTEEQMADL LFAWKVAKHV 

       430        440        450        460        470        480 
KSNAIVYVKD GQTVGVGAGQ MSRVDSATIA GVKAQRMADA MELPESLAKG SAVASDAFFP 

       490        500        510        520 
FADGLMEAAS NGATCVIQPG GSMRDDEVIK AANDAGLAMV FTGMRHFRH 

« Hide

References

[1]"Complete sequence of chromosome of Silicibacter sp. TM1040."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TM1040.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000377 Genomic DNA. Translation: ABF62824.1.
RefSeqYP_612086.1. NC_008044.1.

3D structure databases

ProteinModelPortalQ1GKJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292414.TM1040_0091.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF62824; ABF62824; TM1040_0091.
GeneID4078757.
KEGGsit:TM1040_0091.
PATRIC23384221. VBIRueSp69653_0953.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycRSP292414:GHCT-91-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_RUEST
AccessionPrimary (citable) accession number: Q1GKJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 60 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