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Q5R5C2 (PUR9_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 57. 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):
    5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:ATIC
Synonyms:PURH
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis By similarity.

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.

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

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.

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Subunit structure

Homodimer By similarity.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region.

Sequence similarities

Belongs to the PurH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein PURH
PRO_0000270213

Regions

Nucleotide binding12 – 143IMP By similarity
Nucleotide binding34 – 374IMP By similarity
Nucleotide binding64 – 674IMP By similarity
Nucleotide binding101 – 1044IMP By similarity
Nucleotide binding125 – 1273IMP By similarity
Region207 – 2082AICAR binding By similarity

Sites

Active site1371Proton acceptor Potential
Active site2671Proton acceptor Probable
Binding site3161AICAR; via carbonyl oxygen By similarity
Binding site3391AICAR By similarity
Binding site4311AICAR; shared with dimeric partner By similarity
Binding site4511AICAR; shared with dimeric partner By similarity
Binding site5411AICAR; via carbonyl oxygen; shared with dimeric partner By similarity
Binding site5881AICAR; shared with dimeric partner By similarity
Site2661Transition state stabilizer Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1991N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5C2 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 4991DDFCCD8D0E7B

FASTA59264,693
        10         20         30         40         50         60 
MAPGHLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD VSELTGFPEM 

        70         80         90        100        110        120 
LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA CNLYPFVKTV ASPGVTVEEA 

       130        140        150        160        170        180 
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YVVVSTEMKS SEIKDTSLET RRQLALKAFT 

       190        200        210        220        230        240 
HTAQYDEAIS DYFRKQYSKG ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL 

       250        260        270        280        290        300 
CDALNAWQLV KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS 

       310        320        330        340        350        360 
AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA LKILSKKKNG 

       370        380        390        400        410        420 
NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF SNVVTKNKDL PESALRDLIV 

       430        440        450        460        470        480 
ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS RIHCTRLAGD KANYWWLRHH PQVLSMKFKT 

       490        500        510        520        530        540 
GVKRAEISNA IDQYVTGTIG EDEDLIKWEA LFEEVPELLT EAEKKEWVEK LTEVSISSDA 

       550        560        570        580        590 
FFPFRDNVDR AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860940 mRNA. Translation: CAH93044.1.
RefSeqNP_001126800.1. NM_001133328.1.

3D structure databases

ProteinModelPortalQ5R5C2.
SMRQ5R5C2. Positions 4-592.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R5C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173804.
KEGGpon:100173804.

Organism-specific databases

CTD471.

Phylogenomic databases

HOVERGENHBG006912.
KOK00602.

Enzyme and pathway databases

UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
InterProIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_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_PONAB
AccessionPrimary (citable) accession number: Q5R5C2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 21, 2004
Last modified: October 16, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways