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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
Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (PubMed:25687571).1 Publication

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: 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.

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei137Proton acceptorSequence analysis1
Sitei266Transition state stabilizerSequence analysis1
Active sitei267Proton acceptorCurated1
Binding sitei316AICAR; via carbonyl oxygenBy similarity1
Binding sitei339AICARBy similarity1
Binding sitei431AICAR; shared with dimeric partnerBy similarity1
Binding sitei451AICAR; shared with dimeric partnerBy similarity1
Binding sitei541AICAR; via carbonyl oxygen; shared with dimeric partnerBy similarity1
Binding sitei588AICAR; shared with dimeric partnerBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 14IMPBy similarity3
Nucleotide bindingi34 – 37IMPBy similarity4
Nucleotide bindingi64 – 67IMPBy similarity4
Nucleotide bindingi101 – 104IMPBy similarity4
Nucleotide bindingi125 – 127IMPBy similarity3

GO - Molecular functioni

  • IMP cyclohydrolase activity Source: RGD
  • phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: RGD
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: RGD
  • animal organ regeneration Source: RGD
  • brainstem development Source: RGD
  • cerebellum development Source: RGD
  • cerebral cortex development Source: RGD
  • cobalamin metabolic process Source: RGD
  • dihydrofolate metabolic process Source: RGD
  • nucleoside metabolic process Source: RGD
  • response to inorganic substance Source: RGD
  • ribonucleotide metabolic process Source: RGD
  • tetrahydrofolate biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiR-RNO-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PURH
Cleaved into the following chain:
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
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi70879. Atic.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002702141 – 592Bifunctional purine biosynthesis protein PURHAdd BLAST592
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004343792 – 592Bifunctional purine biosynthesis protein PURH, N-terminally processedAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO35567.
PRIDEiO35567.

PTM databases

iPTMnetiO35567.
PhosphoSitePlusiO35567.

Expressioni

Tissue specificityi

Expressed in liver.1 Publication

Gene expression databases

BgeeiENSRNOG00000015511.
GenevisibleiO35567. RN.

Interactioni

Subunit structurei

Homodimer (By similarity). Associates with internalized INSR complexes on Golgi/endosomal membranes. Interacts with INSR; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling network regulating INSR autophosphorylation and endocytosis (PubMed:25687571).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
InsrP151273EBI-10768817,EBI-10768746

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249543. 1 interactor.
IntActiO35567. 1 interactor.
STRINGi10116.ENSRNOP00000021105.

Structurei

3D structure databases

ProteinModelPortaliO35567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni207 – 208AICAR bindingBy similarity2

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiKOG2555. Eukaryota.
COG0138. LUCA.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiO35567.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG091G03H4.
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. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

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)DescriptionActionsGraphical viewLength
Sequence conflicti24L → H in BAA22837 (PubMed:9332377).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249543. 1 interactor.
IntActiO35567. 1 interactor.
STRINGi10116.ENSRNOP00000021105.

PTM databases

iPTMnetiO35567.
PhosphoSitePlusiO35567.

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

eggNOGiKOG2555. Eukaryota.
COG0138. LUCA.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiO35567.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG091G03H4.
PhylomeDBiO35567.
TreeFamiTF105642.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
ReactomeiR-RNO-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

PROiO35567.

Gene expression databases

BgeeiENSRNOG00000015511.
GenevisibleiO35567. RN.

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. 1 hit.
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...

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: November 30, 2016
This is version 112 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

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 one 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.