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A8FQD4 (PUR9_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:Ssed_0444
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length534 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 – 534534Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076495

Sequences

Sequence LengthMass (Da)Tools
A8FQD4 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: F31C3217A554A2F3

FASTA53457,499
        10         20         30         40         50         60 
MNNARPIRRA LLSVSDKTGI LEFAKSLHAQ GVELLSTGGT ARLLADNGVP VIEVSDHTGH 

        70         80         90        100        110        120 
PEIMDGRVKT LHPKVHGGIL ARRGIDELVM EQNNIKPIDL VAVNLYPFAE TVAKEGCTLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSTAKN HKDTTIIVNA SDYDRVIVEM NANEGSTTLE TRFDLAIAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGTQVPA HSKDECHHDS KFPRTYNTQL VKKQDLRYGE NSHQTAAFYV 

       250        260        270        280        290        300 
DSPSFNGQGD EASVASAIQL QGKALSYNNI ADTDSALECV KEFSEPACVI VKHANPCGVA 

       310        320        330        340        350        360 
IGSDLLDAYN RAFKTDPTSA FGGIIAFNGE LDAATASAIV ERQFVEVIIA PKVSQAARDI 

       370        380        390        400        410        420 
VAAKANLRLL ECGEWNTKTT SLDYKRVNGG LLLQDRDQGM VGLDDVKVVS KRQPTAAEMK 

       430        440        450        460        470        480 
DLMFCWKVAK FVKSNAIVYA KDSMTIGVGA GQMSRVYSAK VAGIKAADEG LEVQDSVMAS 

       490        500        510        520        530 
DAFFPFRDGI DAAAAAGISC IIQPGGSIRD EEIIAAADEH GMAMVFTGMR HFRH 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV35057.1.
RefSeqYP_001472185.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FQD4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING425104.Ssed_0444.

Proteomic databases

PRIDEA8FQD4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV35057; ABV35057; Ssed_0444.
GeneID5612542.
KEGGsse:Ssed_0444.
PATRIC23558098. VBISheSed62411_0465.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycSSED425104:GH7Q-466-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_SHESH
AccessionPrimary (citable) accession number: A8FQD4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 48 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