Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B4S3H9 (PUR9_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:Paes_1700
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length525 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 – 525525Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096081

Sequences

Sequence LengthMass (Da)Tools
B4S3H9 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 1299B42DBDC30A96

FASTA52557,196
        10         20         30         40         50         60 
MSDPVIKRAL VSVSDKTGIV DFCRELGAMG VEIFSTGGTL RILQESGIEA ASISTITGFP 

        70         80         90        100        110        120 
EIMDGRVKTL HPKIHGGLLA VRDNEDHVGQ AKANGIEFID MVVVNLYPFE ATVAKPDVTF 

       130        140        150        160        170        180 
EEAIENIDIG GPSMLRSAAK NNESVTVVTD SADYATVLDE MRSNNGATRR ETRLTLARKV 

       190        200        210        220        230        240 
FELTSRYDRA IADYLIGAEE SGETEAPAAI SVKLEKELDM RYGENPHQSA GFYRLVDGQG 

       250        260        270        280        290        300 
SRCFDDFFDK LHGKELSYNN MLDIAAATGL VEEFRGEDPA VVIIKHTNPC GVAQAGTLVD 

       310        320        330        340        350        360 
AYRKAFSTDT QSPFGGIIAF NVPLDMETAL AVDEIFTEIL IAPAYEDGVL DMLMKKKNRR 

       370        380        390        400        410        420 
LVLQKKALLQ EVMEYKSTQF GMLVQDRDSK IVSREDLKVV TKRQPDEQEL DDMMFAWKIA 

       430        440        450        460        470        480 
KHVKSNTIVY VKNGQTIGVG AGQMSRIDSA KIARSKAAEA GLDIKGSAVA SDAFFPFADG 

       490        500        510        520 
LLAAAEAGAT SVIQPGGSIR DDEVIAAADE NNLAMVFTSM RHFKH 

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
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., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001108 Genomic DNA. Translation: ACF46718.1.
RefSeqYP_002016365.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S3H9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290512.Paes_1700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF46718; ACF46718; Paes_1700.
GeneID6459862.
KEGGpaa:Paes_1700.
PATRIC23043290. VBIProAes37017_1813.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAIRASSKN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPAES290512:GHUT-1745-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_PROA2
AccessionPrimary (citable) accession number: B4S3H9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 43 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