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Protein

Bifunctional purine biosynthesis protein PURH

Gene

Atic

Organism
Rattus norvegicus (Rat)
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.

Pathwayi

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

  1. IMP cyclohydrolase activity Source: RGD
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: RGD
  3. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: RGD
  2. brainstem development Source: RGD
  3. cerebellum development Source: RGD
  4. cerebral cortex development Source: RGD
  5. cobalamin metabolic process Source: RGD
  6. dihydrofolate metabolic process Source: RGD
  7. nucleoside metabolic process Source: RGD
  8. organ regeneration Source: RGD
  9. response to inorganic substance Source: RGD
  10. ribonucleotide metabolic process Source: RGD
  11. tetrahydrofolate biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiREACT_217264. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi70879. Atic.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. membrane Source: Ensembl
  3. mitochondrion Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Bifunctional purine biosynthesis protein PURHPRO_0000270214Add
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

PaxDbiO35567.
PRIDEiO35567.

Expressioni

Tissue specificityi

Expressed in liver.1 Publication

Gene expression databases

GenevestigatoriO35567.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021105.

Structurei

3D structure databases

ProteinModelPortaliO35567.
SMRiO35567. 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.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiO35567.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
PhylomeDBiO35567.
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.

O35567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSQLALFS VSDKTGLVEF ARNLASLGLS LVASGGTAKA IRDAGLAVRD
60 70 80 90 100
VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLIRVVV
110 120 130 140 150
CNLYPFVKTV ASPDVTVEAA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED
160 170 180 190 200
YGAVAAEMQG SGNKDTSLET RRHLALKAFT HTAQYDEAIS DYFRRQYSKG
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
IAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IVAPGYEEEA
360 370 380 390 400
LKILSKKKNG SYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF
410 420 430 440 450
SNIVTKNKDL PESALRDLIV ATIAVKYTQS NSVCYAKDGQ VIGIGAGQQS
460 470 480 490 500
RIHCTRLAGD KANSWWLRHH PRVLSMKFKA GVKRAEVSNA IDQYVTGTIG
510 520 530 540 550
EGEDLVKWKA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA FFPFRDNVDR
560 570 580 590
AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH
Length:592
Mass (Da):64,208
Last modified:January 9, 2007 - v2
Checksum:iD9D710794BB12B95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241L → H in BAA22837 (PubMed:9332377).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89514 mRNA. Translation: BAA22837.1.
BC072496 mRNA. Translation: AAH72496.1.
RefSeqiNP_112276.2. NM_031014.2.
UniGeneiRn.15114.

Genome annotation databases

EnsembliENSRNOT00000021105; ENSRNOP00000021105; ENSRNOG00000015511.
GeneIDi81643.
KEGGirno:81643.
UCSCiRGD:70879. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89514 mRNA. Translation: BAA22837.1.
BC072496 mRNA. Translation: AAH72496.1.
RefSeqiNP_112276.2. NM_031014.2.
UniGeneiRn.15114.

3D structure databases

ProteinModelPortaliO35567.
SMRiO35567. Positions 5-592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021105.

Proteomic databases

PaxDbiO35567.
PRIDEiO35567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021105; ENSRNOP00000021105; ENSRNOG00000015511.
GeneIDi81643.
KEGGirno:81643.
UCSCiRGD:70879. rat.

Organism-specific databases

CTDi471.
RGDi70879. Atic.

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiO35567.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
PhylomeDBiO35567.
TreeFamiTF105642.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
ReactomeiREACT_217264. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi615152.
PROiO35567.

Gene expression databases

GenevestigatoriO35567.

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. "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.

Entry informationi

Entry nameiPUR9_RAT
AccessioniPrimary (citable) accession number: O35567
Secondary accession number(s): Q6IN16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: March 4, 2015
This is version 99 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.