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O35567 (PUR9_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Tissue specificity

Expressed in liver. Ref.1

Domain

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

Sequence similarities

Belongs to the PurH family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Molecular functionHydrolase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from direct assay Ref.1. Source: RGD

brainstem development

Inferred from expression pattern PubMed 7057182. Source: RGD

cerebellum development

Inferred from expression pattern PubMed 7057182. Source: RGD

cerebral cortex development

Inferred from expression pattern PubMed 7057182. Source: RGD

cobalamin metabolic process

Traceable author statement PubMed 3994693. Source: RGD

dihydrofolate metabolic process

Inferred from direct assay PubMed 8948466. Source: RGD

nucleoside metabolic process

Inferred from direct assay PubMed 7370986. Source: RGD

organ regeneration

Inferred from expression pattern Ref.1. Source: RGD

response to inorganic substance

Inferred from expression pattern PubMed 4078017. Source: RGD

ribonucleotide metabolic process

Inferred from direct assay PubMed 4078017. Source: RGD

tetrahydrofolate biosynthetic process

Inferred from direct assay PubMed 7057182. Source: RGD

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionIMP cyclohydrolase activity

Inferred from direct assay Ref.1. Source: RGD

phosphoribosylaminoimidazolecarboxamide formyltransferase activity

Inferred from direct assay Ref.1. Source: RGD

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein PURH
PRO_0000270214

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

Experimental info

Sequence conflict241L → H in BAA22837. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35567 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: D9D710794BB12B95

FASTA59264,208
        10         20         30         40         50         60 
MASSQLALFS VSDKTGLVEF ARNLASLGLS LVASGGTAKA IRDAGLAVRD VSELTGFPEM 

        70         80         90        100        110        120 
LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLIRVVV CNLYPFVKTV ASPDVTVEAA 

       130        140        150        160        170        180 
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YGAVAAEMQG SGNKDTSLET RRHLALKAFT 

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

       250        260        270        280        290        300 
CDALNAWQLV TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA 

       310        320        330        340        350        360 
IAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IVAPGYEEEA LKILSKKKNG 

       370        380        390        400        410        420 
SYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF SNIVTKNKDL PESALRDLIV 

       430        440        450        460        470        480 
ATIAVKYTQS NSVCYAKDGQ VIGIGAGQQS RIHCTRLAGD KANSWWLRHH PRVLSMKFKA 

       490        500        510        520        530        540 
GVKRAEVSNA IDQYVTGTIG EGEDLVKWKA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA 

       550        560        570        580        590 
FFPFRDNVDR AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a rat cDNA encoding 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase."
Akira T., Komatsu M., Nango R., Tomooka A., Konaka K., Yamauchi M., Kitamura Y., Nomura S., Tsukamoto I.
Gene 197:289-293(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: Donryu.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[3]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 178-194; 531-545 AND 570-588, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89514 mRNA. Translation: BAA22837.1.
BC072496 mRNA. Translation: AAH72496.1.
RefSeqNP_112276.2. NM_031014.2.
UniGeneRn.15114.

3D structure databases

ProteinModelPortalO35567.
SMRO35567. Positions 5-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021105.

Proteomic databases

PaxDbO35567.
PRIDEO35567.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021105; ENSRNOP00000021105; ENSRNOG00000015511.
GeneID81643.
KEGGrno:81643.
UCSCRGD:70879. rat.

Organism-specific databases

CTD471.
RGD70879. Atic.

Phylogenomic databases

eggNOGCOG0138.
GeneTreeENSGT00390000004553.
HOGENOMHOG000230372.
HOVERGENHBG006912.
InParanoidO35567.
KOK00602.
OMADLLFAWK.
OrthoDBEOG74N5GD.
PhylomeDBO35567.
TreeFamTF105642.

Enzyme and pathway databases

UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Gene expression databases

GenevestigatorO35567.

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...

Other

NextBio615152.
PROO35567.

Entry information

Entry namePUR9_RAT
AccessionPrimary (citable) accession number: O35567
Secondary accession number(s): Q6IN16
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 93 of the entry and version 2 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