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C4LA41 (PUR9_TOLAT) 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:Tola_0541
OrganismTolumonas auensis (strain DSM 9187 / TA4) [Complete proteome] [HAMAP]
Taxonomic identifier595494 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeTolumonas

Protein attributes

Sequence length530 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 – 530530Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000203255

Sequences

Sequence LengthMass (Da)Tools
C4LA41 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 666614F6C764A14B

FASTA53057,280
        10         20         30         40         50         60 
MENARPIRRA LLSVSDKTGI VEFARALQQR GVELLSTGGT ARLLADAGLA VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRNTDDAIM TQHGIKPIDL VAVNLYPFAA TVANPDCALE 

       130        140        150        160        170        180 
DAIENIDIGG PTMVRSAAKN HKDVTIVVNA KDYTRVLAEM DANANSLTYT TRFDLAIAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGTKVPT YGVQDEASAD SKFPRTINFQ FIKKQDMRYG ENSHQAAAFY 

       250        260        270        280        290        300 
VEADVKEASV STATQLQGKA LSYNNIADTD AALECVKEFA EPACVIVKHA NPCGVALGND 

       310        320        330        340        350        360 
ILEAYNRAYQ TDPTSAFGGI IAFNRELDAA TAEAIVSRQF VEVIIAPVVS EEAKAVVAKK 

       370        380        390        400        410        420 
ANVRLLECGQ WQGKANGFDV KRVNGGLLVQ DRDQGMVTLT DLKVVTKRQP TEQELKDLLF 

       430        440        450        460        470        480 
CWKVGKFVKS NAIVYAKDSM TIGVGAGQMS RVYSAKIAGI KAADEGLEVK GSVMASDAFF 

       490        500        510        520        530 
PFRDGIDAAA EAGITCVIQP GGSMRDQEVI DAADEHGMAM VFTNMRHFRH 

« Hide

References

[1]"Complete sequence of Tolumonas auensis DSM 9187."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S., Beller H.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9187 / TA4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001616 Genomic DNA. Translation: ACQ92170.1.
RefSeqYP_002891756.1. NC_012691.1.

3D structure databases

ProteinModelPortalC4LA41.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595494.Tola_0541.

Proteomic databases

PRIDEC4LA41.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ92170; ACQ92170; Tola_0541.
GeneID7883356.
KEGGtau:Tola_0541.
PATRIC23977685. VBITolAue42623_0545.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycTAUE595494:GHEF-564-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_TOLAT
AccessionPrimary (citable) accession number: C4LA41
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
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