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O67775 (PUR9_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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:aq_1963
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length506 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 506506Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192068

Sequences

Sequence LengthMass (Da)Tools
O67775 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 46998C8B1B1FE694

FASTA50656,677
        10         20         30         40         50         60 
MRAIISVYRK EGIDKLAKAL QELGYEIVST GGTAKYLREK GISVKEVSEI TGFPEILEGR 

        70         80         90        100        110        120 
VKTLHPVVHG GILFRDWVEK DKEEIEKHGI KPIDVVVVNL YPFEEKLKEG LTDKDLMEFI 

       130        140        150        160        170        180 
DIGGPTLIRA AAKNFFRVVI LVDPEDYDWV IEKLKKGNLT LQDRAYLAWK AFSHTAYYDG 

       190        200        210        220        230        240 
VISQAFKKLY SIDTFGKEEA LPLKRMQKLR YGENPHQRGF LYENPLEDIG ITKAQVLQGK 

       250        260        270        280        290        300 
EMSFNNYLDA DSAVRLVAEF PNQTVCAIIK HNNPCGVALG SSVKEAFLRA KEADPVSAFG 

       310        320        330        340        350        360 
GIVAFNDKVD GETAKELTSM FLEVVIAPDY DEEALRELSR KKNLRVIRFF GFQHAFDVKK 

       370        380        390        400        410        420 
VSGGYLLQDE DTVLYEKLQV VTKREPTAEE MEDLLFAWKV VKHTKSNAVV IAKNGQTLGI 

       430        440        450        460        470        480 
GSGNVSRVDS LKCAINKAKE FGFDLKGAVV ASEAFFPFRD SIDIMAKEGI TAVIQPGGSI 

       490        500 
RDQEVIDACN EHGIAMIFTG LRHFKH 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07734.1.
PIRC70468.
RefSeqNP_214344.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67775.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1963.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07734; AAC07734; aq_1963.
GeneID1193672.
KEGGaae:aq_1963.
PATRIC20960838. VBIAquAeo85532_1514.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1405-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_AQUAE
AccessionPrimary (citable) accession number: O67775
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 90 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