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A9BIX9 (PUR9_PETMO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:Pmob_1777
OrganismPetrotoga mobilis (strain DSM 10674 / SJ95) [Complete proteome] [HAMAP]
Taxonomic identifier403833 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaePetrotoga

Protein attributes

Sequence length508 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 – 508508Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076487

Sequences

Sequence LengthMass (Da)Tools
A9BIX9 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 99BFEB1EFF966C0E

FASTA50857,068
        10         20         30         40         50         60 
MIKRALLSTY KKEKVVDFAQ TLQELGIEII STGGTAKKLQ ENSIEVTPVE EITNFPEILN 

        70         80         90        100        110        120 
GRVKTLNPFI QGGILARREN KQDMETLENL KIEPIDLIYV NLYPFVEVAN KRDVDMNELI 

       130        140        150        160        170        180 
EFIDIGGPTM IRSAAKNYKD VIVVVDESDL EQISAKLKTP EELDENYRLY LASKAFNLTA 

       190        200        210        220        230        240 
FYDSCISNYL NAQLTNKDDF QEFLTVPFEK SYEMRYGENP HQSAIFYKNT LTSGAMTSFE 

       250        260        270        280        290        300 
QLNGKELSFN NLRDADSAWK AVNEFEDTAC CCLKHSSPCG IALGDSVIEA YQKAYSCDPV 

       310        320        330        340        350        360 
SIFGGIVAFN RKIDVETALE LKKIFLEIIM APEYDEEALD ILKEKKNLRI LKMNSKPIDT 

       370        380        390        400        410        420 
YEYVSVDGGI LVQEVDKRVI NEFEVVTETK VSEEIKEELL FAWKAVKHVK SNAIVVSKNK 

       430        440        450        460        470        480 
ATTGIGAGQP NRIWAATQAL ERSKDKGGDV LASDAFFPFS DVVEKAAEYG IKAIIQPGGS 

       490        500 
IRDDESIQAC SKYGIAMVFT GMRHFKHI 

« Hide

References

[1]"Complete sequence of Petroga mobilis SJ95."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Noll K., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 10674 / SJ95.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000879 Genomic DNA. Translation: ABX32467.1.
RefSeqYP_001568790.1. NC_010003.1.

3D structure databases

ProteinModelPortalA9BIX9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING403833.Pmob_1777.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX32467; ABX32467; Pmob_1777.
GeneID5757923.
KEGGpmo:Pmob_1777.
PATRIC22921380. VBIPetMob40494_1902.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPMOB403833:GH51-1824-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_PETMO
AccessionPrimary (citable) accession number: A9BIX9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 45 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