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A3QII0 (PUR9_SHELP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Shew_3412
OrganismShewanella loihica (strain ATCC BAA-1088 / PV-4) [Complete proteome] [HAMAP]
Taxonomic identifier323850 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length529 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 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018953

Sequences

Sequence LengthMass (Da)Tools
A3QII0 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: DD4D7F174D03893E

FASTA52957,226
        10         20         30         40         50         60 
MNNARPIRRA LLSVSDKTGI LEFAQALHAQ GVELLSTGGT ARLLADNGVP VIEVSDYTGH 

        70         80         90        100        110        120 
PEIMDGRVKT LHPKVHGGIL GRRGIDEIVM EQNAIKPIDL VAVNLYPFAE TVAKEGCTLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSTAKN HKDTTIVVNA KDYDRVIQEM QANQGSTTLE TRFDLAIAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGTMVPA HSQDECHQDS KFPRTYNTQL VKKQDLRYGE NSHQSAAFYV 

       250        260        270        280        290        300 
DLNIDEASVA SATQLQGKAL SYNNIADTDA ALECVKEFSE PACVIVKHAN PCGVAIGKDL 

       310        320        330        340        350        360 
LEAYNRAYQT DPTSAFGGII AFNGELDAET ASAIVERQFV EVIIAPVVSQ AARDVVAAKA 

       370        380        390        400        410        420 
NVRLLECGQW ASKTRSLDYK RVNGGLLIQD RDQGMVEMSD IKVVTKRQPT EAEMKDLMFC 

       430        440        450        460        470        480 
WKVAKFVKSN AIVYAKDSMT IGVGAGQMSR VYSAKVAGIK AADENLEVVG SVMASDAFFP 

       490        500        510        520 
FRDGIDAAAA AGISCIIQPG GSIRDEEIIA AADEHGMAMV FTGMRHFRH 

« Hide

References

[1]"Complete sequence of Shewanella loihica PV-4."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G., Fredrickson J., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1088 / PV-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000606 Genomic DNA. Translation: ABO25278.1.
RefSeqYP_001095537.1. NC_009092.1.

3D structure databases

ProteinModelPortalA3QII0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323850.Shew_3412.

Proteomic databases

PRIDEA3QII0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO25278; ABO25278; Shew_3412.
GeneID4923566.
KEGGslo:Shew_3412.
PATRIC23518749. VBISheLoi132094_3412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSLOI323850:GHQJ-3519-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_SHELP
AccessionPrimary (citable) accession number: A3QII0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 52 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