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Reviewed, UniProtKB/Swiss-Prot Q0VCK0 (PUR9_BOVIN)

Last modified February 9, 2010. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein PURH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: ATIC
Synonyms: PURH
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

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

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein PURH
PRO_0000270212

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 residue1041Phosphotyrosine By similarity
Modified residue1991N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q0VCK0-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: EBD94993555935D7

FASTA59264,483
        10         20         30         40         50         60 
MAPGQLALFS VSDKNGLVEF ARNLASVGLN LIASGGTAKA LRDAGLAVRD VSELTGFPEM 

        70         80         90        100        110        120 
LGGRVKTLHP AVHAGILARD IPEDSADMAK LDFNLIRVVV CNLYPFGKTV ASPGVTVEEA 

       130        140        150        160        170        180 
VEHIDIGGVT LLRAAAKNHA RVTVVCEPED YAAVASEMQD SDSKDTSLET RRQLALKAFT 

       190        200        210        220        230        240 
HTAQYDEAIS DYFRKEYSKG VSQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL 

       250        260        270        280        290        300 
CDALNAWQLV KELKEALGLP AAASFKHVSP AGAAVGIPLS EDEANVCMVY DLYKTLTPVA 

       310        320        330        340        350        360 
TAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYENEA LKILSKKKNG 

       370        380        390        400        410        420 
NYCVLQMDQS YIPDENEVRT LFGLRLSQKR NNSVVNRSLF SNIVTKNKDL PESALRDLIV 

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

       490        500        510        520        530        540 
GVKRAEISNA IDQYVTGTIG EGEDLIKWKA LFEEVPELLT ETEKKEWIDK LNEVSISSDA 

       550        560        570        580        590 
FFPFRDNVDR AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH

« Hide

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References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal lung.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC120131 mRNA. Translation: AAI20132.1.
IPIIPI00724051.
RefSeqNP_001068722.1.
UniGeneBt.61076

3D structure databases

SMRQ0VCK0. Positions 4-592.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0VCK0.

Genome annotation databases

EnsemblENSBTAT00000052629; ENSBTAP00000048873; ENSBTAG00000019274; Bos taurus. [Genome view]
GeneID506343.
KEGGbta:506343.

Organism-specific databases

CTD506343.

Phylogenomic databases

eggNOGmaNOG06996.
HOVERGENQ0VCK0.
InParanoidQ0VCK0.
PhylomeDBQ0VCK0.

Enzyme and pathway databases

BRENDA2.1.2.3. 251.
3.5.4.10. 251.

Family and domain databases

InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHase_bienz.
IPR011607. MGS.
[Graphical view]
PANTHERPTHR11692. AICARFT_IMPCHas. 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]
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

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Entry information

Entry namePUR9_BOVIN
AccessionPrimary (citable) accession number: Q0VCK0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: September 5, 2006
Last modified: February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents