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Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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:iIMP 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:iIMP 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_321076. 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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Bifunctional purine biosynthesis protein PURHPRO_0000270212Add
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

PaxDbiQ0VCK0.
PRIDEiQ0VCK0.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000025662.

Structurei

3D structure databases

ProteinModelPortaliQ0VCK0.
SMRiQ0VCK0. Positions 4-592.
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.
InParanoidiQ0VCK0.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
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.

Q0VCK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPGQLALFS VSDKNGLVEF ARNLASVGLN LIASGGTAKA LRDAGLAVRD
60 70 80 90 100
VSELTGFPEM LGGRVKTLHP AVHAGILARD IPEDSADMAK LDFNLIRVVV
110 120 130 140 150
CNLYPFGKTV ASPGVTVEEA VEHIDIGGVT LLRAAAKNHA RVTVVCEPED
160 170 180 190 200
YAAVASEMQD SDSKDTSLET RRQLALKAFT HTAQYDEAIS DYFRKEYSKG
210 220 230 240 250
VSQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL CDALNAWQLV
260 270 280 290 300
KELKEALGLP AAASFKHVSP AGAAVGIPLS EDEANVCMVY DLYKTLTPVA
310 320 330 340 350
TAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYENEA
360 370 380 390 400
LKILSKKKNG NYCVLQMDQS YIPDENEVRT LFGLRLSQKR NNSVVNRSLF
410 420 430 440 450
SNIVTKNKDL PESALRDLIV ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS
460 470 480 490 500
RIHCTRLAGD KANCWWLRHH PQVLSMKFKT GVKRAEISNA IDQYVTGTIG
510 520 530 540 550
EGEDLIKWKA LFEEVPELLT ETEKKEWIDK LNEVSISSDA FFPFRDNVDR
560 570 580 590
AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH
Length:592
Mass (Da):64,483
Last modified:September 5, 2006 - v1
Checksum:iEBD94993555935D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120131 mRNA. Translation: AAI20132.1.
RefSeqiNP_001068722.1. NM_001075254.2.
UniGeneiBt.61076.

Genome annotation databases

EnsembliENSBTAT00000025662; ENSBTAP00000025662; ENSBTAG00000019274.
GeneIDi506343.
KEGGibta:506343.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120131 mRNA. Translation: AAI20132.1.
RefSeqiNP_001068722.1. NM_001075254.2.
UniGeneiBt.61076.

3D structure databases

ProteinModelPortaliQ0VCK0.
SMRiQ0VCK0. Positions 4-592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000025662.

Proteomic databases

PaxDbiQ0VCK0.
PRIDEiQ0VCK0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000025662; ENSBTAP00000025662; ENSBTAG00000019274.
GeneIDi506343.
KEGGibta:506343.

Organism-specific databases

CTDi471.

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiQ0VCK0.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
TreeFamiTF105642.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
ReactomeiREACT_321076. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi20867570.

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

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal lung.

Entry informationi

Entry nameiPUR9_BOVIN
AccessioniPrimary (citable) accession number: Q0VCK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: September 5, 2006
Last modified: June 24, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.