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Protein

Bifunctional purine biosynthesis protein PURH

Gene

Atic

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 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).
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PURH (Atic)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 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), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathway: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PURH (Atic)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei137 – 1371Proton acceptorSequence Analysis
Sitei266 – 2661Transition state stabilizerSequence Analysis
Active sitei267 – 2671Proton acceptorCurated
Binding sitei316 – 3161AICAR; via carbonyl oxygenBy similarity
Binding sitei339 – 3391AICARBy similarity
Binding sitei431 – 4311AICAR; shared with dimeric partnerBy similarity
Binding sitei451 – 4511AICAR; shared with dimeric partnerBy similarity
Binding sitei541 – 5411AICAR; via carbonyl oxygen; shared with dimeric partnerBy similarity
Binding sitei588 – 5881AICAR; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 143IMPBy similarity
Nucleotide bindingi34 – 374IMPBy similarity
Nucleotide bindingi64 – 674IMPBy similarity
Nucleotide bindingi101 – 1044IMPBy similarity
Nucleotide bindingi125 – 1273IMPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiREACT_344602. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PURH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:Atic
Synonyms:Purh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1351352. Atic.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Bifunctional purine biosynthesis protein PURHPRO_0000192157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CWJ9.
PaxDbiQ9CWJ9.
PRIDEiQ9CWJ9.

2D gel databases

REPRODUCTION-2DPAGEQ9CWJ9.

PTM databases

PhosphoSiteiQ9CWJ9.

Expressioni

Gene expression databases

BgeeiQ9CWJ9.
ExpressionAtlasiQ9CWJ9. baseline and differential.
GenevisibleiQ9CWJ9. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi223864. 1 interaction.
IntActiQ9CWJ9. 2 interactions.
MINTiMINT-1855853.
STRINGi10090.ENSMUSP00000027384.

Structurei

3D structure databases

ProteinModelPortaliQ9CWJ9.
SMRiQ9CWJ9. Positions 5-592.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 2082AICAR bindingBy similarity

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOVERGENiHBG006912.
InParanoidiQ9CWJ9.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
PhylomeDBiQ9CWJ9.
TreeFamiTF105642.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CWJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSQLALFS VSDKTGLVEF ARSLASLGLS LVASGGTAKA IRDAGLAVRD
60 70 80 90 100
VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLVRVVV
110 120 130 140 150
CNLYPFVKTV ASPDVTVEAA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED
160 170 180 190 200
YAGVAAEMHG SDSKDTSLET RRHLALKAFT HTAQYDEAIS DYFRKQYSKG
210 220 230 240 250
ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL CDALNAWQLV
260 270 280 290 300
TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA
310 320 330 340 350
VAYARARGAD RMSSFGDFVA LSDICDVPTA KIISREVSDG IVAPGYEEEA
360 370 380 390 400
LKILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF
410 420 430 440 450
SNIVTKNKDL PESALRDLIV ATVAVKYTQS NSVCYAKDGQ VIGIGAGQQS
460 470 480 490 500
RIHCTRLAGD KANSWWLRHH PRVLSMKFKA GVKRAEISNA IDQYVTGTIG
510 520 530 540 550
EGEDLVKWEA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA FFPFRDNVDR
560 570 580 590
AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH
Length:592
Mass (Da):64,217
Last modified:May 1, 2007 - v2
Checksum:i8C5278040059FB5D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221R → K in BAB26949 (PubMed:16141072).Curated
Sequence conflicti183 – 1831A → T in BAE23927 (PubMed:16141072).Curated
Sequence conflicti219 – 2191L → S in AAH39925 (PubMed:15489334).Curated
Sequence conflicti371 – 3711Y → C in BAB27060 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15030.1.
RefSeqiNP_080471.2. NM_026195.3.
UniGeneiMm.38010.

Genome annotation databases

EnsembliENSMUST00000027384; ENSMUSP00000027384; ENSMUSG00000026192.
GeneIDi108147.
KEGGimmu:108147.
UCSCiuc007bjs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15030.1.
RefSeqiNP_080471.2. NM_026195.3.
UniGeneiMm.38010.

3D structure databases

ProteinModelPortaliQ9CWJ9.
SMRiQ9CWJ9. Positions 5-592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223864. 1 interaction.
IntActiQ9CWJ9. 2 interactions.
MINTiMINT-1855853.
STRINGi10090.ENSMUSP00000027384.

Chemistry

BindingDBiQ9CWJ9.
ChEMBLiCHEMBL2277.

PTM databases

PhosphoSiteiQ9CWJ9.

2D gel databases

REPRODUCTION-2DPAGEQ9CWJ9.

Proteomic databases

MaxQBiQ9CWJ9.
PaxDbiQ9CWJ9.
PRIDEiQ9CWJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027384; ENSMUSP00000027384; ENSMUSG00000026192.
GeneIDi108147.
KEGGimmu:108147.
UCSCiuc007bjs.2. mouse.

Organism-specific databases

CTDi471.
MGIiMGI:1351352. Atic.

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOVERGENiHBG006912.
InParanoidiQ9CWJ9.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
PhylomeDBiQ9CWJ9.
TreeFamiTF105642.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
ReactomeiREACT_344602. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

ChiTaRSiAtic. mouse.
NextBioi360158.
PROiQ9CWJ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CWJ9.
ExpressionAtlasiQ9CWJ9. baseline and differential.
GenevisibleiQ9CWJ9. MM.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.

Entry informationi

Entry nameiPUR9_MOUSE
AccessioniPrimary (citable) accession number: Q9CWJ9
Secondary accession number(s): Q3UTQ3
, Q80UH0, Q8BPF0, Q8BQV9, Q9CRI1, Q9CZW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2007
Last modified: June 24, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.