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Q9CWJ9 (PUR9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

Domain

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

Sequence similarities

Belongs to the PurH family.

Sequence caution

The sequence BAB28011.1 differs from that shown. Reason: Frameshift at position 558.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein PURH
PRO_0000192157

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 residue1991N6-acetyllysine By similarity

Experimental info

Sequence conflict221R → K in BAB26949. Ref.1
Sequence conflict1831A → T in BAE23927. Ref.1
Sequence conflict2191L → S in AAH39925. Ref.2
Sequence conflict3711Y → C in BAB27060. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CWJ9 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 8C5278040059FB5D

FASTA59264,217
        10         20         30         40         50         60 
MAPSQLALFS VSDKTGLVEF ARSLASLGLS LVASGGTAKA IRDAGLAVRD VSELTGFPEM 

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

       130        140        150        160        170        180 
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YAGVAAEMHG SDSKDTSLET RRHLALKAFT 

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

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

       310        320        330        340        350        360 
VAYARARGAD RMSSFGDFVA LSDICDVPTA KIISREVSDG IVAPGYEEEA LKILSKKKNG 

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

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

       490        500        510        520        530        540 
GVKRAEISNA IDQYVTGTIG EGEDLVKWEA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA 

       550        560        570        580        590 
FFPFRDNVDR AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Corpora quadrigemina and Embryonic stem cell.
[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].
Strain: 129.
Tissue: Mammary tumor.
[3]Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 98-108; 178-194 AND 531-545, MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK010449 mRNA. Translation: BAB26949.3.
AK010611 mRNA. Translation: BAB27060.1.
AK012074 mRNA. Translation: BAB28011.1. Frameshift.
AK046353 mRNA. Translation: BAC32688.1.
AK076091 mRNA. Translation: BAC36175.1.
AK139235 mRNA. Translation: BAE23927.1.
BC039925 mRNA. Translation: AAH39925.2.
IPIIPI00330303.
RefSeqNP_080471.2. NM_026195.3.
UniGeneMm.38010.

3D structure databases

ProteinModelPortalQ9CWJ9.
SMRQ9CWJ9. Positions 5-592.
ModBaseSearch...

PTM databases

PhosphoSiteQ9CWJ9.

2D gel databases

REPRODUCTION-2DPAGEQ9CWJ9.

Proteomic databases

PaxDbQ9CWJ9.
PRIDEQ9CWJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027384; ENSMUSP00000027384; ENSMUSG00000026192.
GeneID108147.
KEGGmmu:108147.
UCSCuc007bjs.2. mouse.

Organism-specific databases

CTD471.
MGIMGI:1351352. Atic.

Phylogenomic databases

eggNOGCOG0138.
GeneTreeENSGT00390000004553.
HOVERGENHBG006912.
InParanoidQ9CWJ9.
KOK00602.
OMADLLFAWK.
OrthoDBEOG43BMNG.

Enzyme and pathway databases

UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Gene expression databases

ArrayExpressQ9CWJ9.
BgeeQ9CWJ9.
GenevestigatorQ9CWJ9.
GermOnlineENSMUSG00000026192. Mus musculus.

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]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Other

BindingDBQ9CWJ9.
ChEMBLCHEMBL2277.
ChiTaRSATIC. mouse.
NextBio360158.
SOURCESearch...

Entry information

Entry namePUR9_MOUSE
AccessionPrimary (citable) accession number: Q9CWJ9
Secondary accession number(s): Q3UTQ3 expand/collapse secondary AC list , Q80UH0, Q8BPF0, Q8BQV9, Q9CRI1, Q9CZW9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2007
Last modified: April 3, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents