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B8I490 (PUR9_CLOCE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:Ccel_2181
OrganismClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]
Taxonomic identifier394503 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length514 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 – 514514Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122953

Sequences

Sequence LengthMass (Da)Tools
B8I490 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 5EBEFA92D4FF94F6

FASTA51456,148
        10         20         30         40         50         60 
MIKRALISVS DKTGIVEFAS ALASKGIEII STGGTAKALS AAGLKVINIS DITGFPECLD 

        70         80         90        100        110        120 
GRVKTLHPKV HAGLLAIRSN EEHMKQIKEL GVETIDMVII NLYPFKQTIL KGNVELEEAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRAAAKNYQD VAVIVDPADY KNVLNEMNES GDVSVKTKFR LAYKVFEHTS 

       190        200        210        220        230        240 
HYDTLIAKYL RDTLGDIDFP ETLSLTYEKA QDMRYGENPH QKAVFYKEVG ANTGLLPSAV 

       250        260        270        280        290        300 
QLHGKELSFN NINDTNGAIE LVKEFDEPTV VAVKHTNPCG VGSADNIYDA YMRAYESDPV 

       310        320        330        340        350        360 
SIFGGIIAAN REIDAKTAEE INKIFVEIVV APSFTEDALA VLTQKKNVRL LKLENITDEI 

       370        380        390        400        410        420 
SPDAYDMKKV AGGLLVQKYN SQLFNQEDLK CVTDVQPTKE QMEDLVFAMK VVKHTKSNAI 

       430        440        450        460        470        480 
TLAKGKMTIG VGPGQTNRIV PTKVSIEYAG ERSQGAVMAS DAYFPFSDCV EAAAAAGIKA 

       490        500        510 
IIQPGGSIRD QESIDACNKY GIAMVFTGMR HFKH 

« Hide

References

[1]"Complete sequence of Clostridium cellulolyticum H10."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ivanova N., Zhou J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001348 Genomic DNA. Translation: ACL76523.1.
RefSeqYP_002506503.1. NC_011898.1.

3D structure databases

ProteinModelPortalB8I490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394503.Ccel_2181.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL76523; ACL76523; Ccel_2181.
GeneID7310871.
KEGGcce:Ccel_2181.
PATRIC19435289. VBICloCel57783_2243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAGIGQADN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCCEL394503:GJET-2227-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_CLOCE
AccessionPrimary (citable) accession number: B8I490
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 39 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