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B1KNA0 (PUR9_SHEWM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:Swoo_0296
OrganismShewanella woodyi (strain ATCC 51908 / MS32) [Complete proteome] [HAMAP]
Taxonomic identifier392500 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length535 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 – 535535Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096096

Sequences

Sequence LengthMass (Da)Tools
B1KNA0 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 4446705B9A63A128

FASTA53557,881
        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 HDYDRVIAEM EANQGSTTLE TRFDLAIAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGTKVPA HSQDECHERS LCAEDSKFPR TYNTQLVKKQ DLRYGENSHQ 

       250        260        270        280        290        300 
TAAFYVDTNI DEASVATAVQ LQGKALSYNN IADTDSALEC VKEFSEPACV IVKHANPCGV 

       310        320        330        340        350        360 
AIGENLLEAY NRAFQTDPTS AFGGIIAFNA ELDAETAAAI VERQFVEVII APKVCQAARD 

       370        380        390        400        410        420 
VVAAKANVRL LECGEWANKT TSLDYKRVNG GLLLQDRDQG MVGLDEVKVV SKRQPTEAEM 

       430        440        450        460        470        480 
KDLMFCWKVA KFVKSNAIVY AKNSMTIGVG AGQMSRVYSA KVAGIKAADE GLEVQDSVMA 

       490        500        510        520        530 
SDAFFPFRDG IDAAAAAGIS CIIQPGGSIR DEEIIAAADE HGMAMVFTGM RHFRH 

« Hide

References

[1]"Complete sequence of Shewanella woodyi ATCC 51908."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51908 / MS32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000961 Genomic DNA. Translation: ACA84597.1.
RefSeqYP_001758692.1. NC_010506.1.

3D structure databases

ProteinModelPortalB1KNA0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING392500.Swoo_0296.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA84597; ACA84597; Swoo_0296.
GeneID6114522.
KEGGswd:Swoo_0296.
PATRIC23602803. VBISheWoo126588_0305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSWOO392500:GI2C-305-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_SHEWM
AccessionPrimary (citable) accession number: B1KNA0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 44 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