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Q12IP4 (PUR9_SHEDO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:Sden_3407
OrganismShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [Complete proteome] [HAMAP]
Taxonomic identifier318161 [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_1000018951

Sequences

Sequence LengthMass (Da)Tools
Q12IP4 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 3A8A98B790C40A57

FASTA53457,417
        10         20         30         40         50         60 
MNTVRPIRRA LLSVSDKTGI LEFAQALHAH GVELLSTGGT ARLLAEHGLP VIEASDHTGH 

        70         80         90        100        110        120 
PEIMDGRVKT LHPKIHGGIL ARRGQDEAVM AENNILPIDL VVVNLYPFAS TVANPDCTLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRAAAKN HQDVTIVVNA SDYARVLAEM KTNQGSTTLK IRFELAVAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGNLVAM DADTSDEQQA LHQESSFPRT FNSQFIKKQD LRYGENSHQK 

       250        260        270        280        290        300 
AAFYVDPQID EASVASAIQL QGKALSYNNI ADTDAALECV KEFDGPACVI VKHANPCGVA 

       310        320        330        340        350        360 
LGKDLLDAYN RAYQTDPTSA FGGIIAFNGE LDAATASAIV ERQFVEVIIA PSVSQAARDI 

       370        380        390        400        410        420 
VAAKANVRLL ECGKWETKTT SLDYKRVNGG LLVQDRDQGM VGLADIKVVS KRQPTEAELK 

       430        440        450        460        470        480 
DLLFCWKVAK FVKSNAIVYA KEGMTIGVGA GQMSRVYSAK IAGIKASDEG LVVENSVMAS 

       490        500        510        520        530 
DAFFPFRDGI DAAAAAGISC IIQPGGSIRD EEIIKAADEH GMAMVFTGMR HFRH 

« Hide

References

[1]"Complete sequence of Shewanella denitrificans OS217."
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., Gilna P., Kiss H., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS217 / ATCC BAA-1090 / DSM 15013.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000302 Genomic DNA. Translation: ABE56682.1.
RefSeqYP_564405.1. NC_007954.1.

3D structure databases

ProteinModelPortalQ12IP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318161.Sden_3407.

Proteomic databases

PRIDEQ12IP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE56682; ABE56682; Sden_3407.
GeneID4019955.
KEGGsdn:Sden_3407.
PATRIC23492906. VBISheDen79529_3577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSDEN318161:GHKQ-3520-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_SHEDO
AccessionPrimary (citable) accession number: Q12IP4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 59 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