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O35567

- PUR9_RAT

UniProt

O35567 - PUR9_RAT

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Protein
Bifunctional purine biosynthesis protein PURH
Gene
Atic, Purh
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 acceptor Reviewed prediction
Sitei266 – 2661Transition state stabilizer Reviewed prediction
Active sitei267 – 2671Proton acceptor Inferred
Binding sitei316 – 3161AICAR; via carbonyl oxygen By similarity
Binding sitei339 – 3391AICAR By similarity
Binding sitei431 – 4311AICAR; shared with dimeric partner By similarity
Binding sitei451 – 4511AICAR; shared with dimeric partner By similarity
Binding sitei541 – 5411AICAR; via carbonyl oxygen; shared with dimeric partner By similarity
Binding sitei588 – 5881AICAR; shared with dimeric partner By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 143IMP By similarity
Nucleotide bindingi34 – 374IMP By similarity
Nucleotide bindingi64 – 674IMP By similarity
Nucleotide bindingi101 – 1044IMP By similarity
Nucleotide bindingi125 – 1273IMP By 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. mitochondrion Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Bifunctional purine biosynthesis protein PURH
PRO_0000270214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei199 – 1991N6-acetyllysine By 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.

Family & Domainsi

Region

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

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiO35567.
KOiK00602.
OMAiAGDKANC.
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.
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

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MASSQLALFS VSDKTGLVEF ARNLASLGLS LVASGGTAKA IRDAGLAVRD    50
VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLIRVVV 100
CNLYPFVKTV ASPDVTVEAA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED 150
YGAVAAEMQG SGNKDTSLET RRHLALKAFT HTAQYDEAIS DYFRRQYSKG 200
ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL CDALNAWQLV 250
TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA 300
IAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IVAPGYEEEA 350
LKILSKKKNG SYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF 400
SNIVTKNKDL PESALRDLIV ATIAVKYTQS NSVCYAKDGQ VIGIGAGQQS 450
RIHCTRLAGD KANSWWLRHH PRVLSMKFKA GVKRAEVSNA IDQYVTGTIG 500
EGEDLVKWKA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA FFPFRDNVDR 550
AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH 592
Length:592
Mass (Da):64,208
Last modified:January 9, 2007 - v2
Checksum:iD9D710794BB12B95
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241L → H in BAA22837. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D89514 mRNA. Translation: BAA22837.1 .
BC072496 mRNA. Translation: AAH72496.1 .
RefSeqi NP_112276.2. NM_031014.2.
UniGenei Rn.15114.

3D structure databases

ProteinModelPortali O35567.
SMRi O35567. Positions 5-592.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021105.

Proteomic databases

PaxDbi O35567.
PRIDEi O35567.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021105 ; ENSRNOP00000021105 ; ENSRNOG00000015511 .
GeneIDi 81643.
KEGGi rno:81643.
UCSCi RGD:70879. rat.

Organism-specific databases

CTDi 471.
RGDi 70879. Atic.

Phylogenomic databases

eggNOGi COG0138.
GeneTreei ENSGT00390000004553.
HOGENOMi HOG000230372.
HOVERGENi HBG006912.
InParanoidi O35567.
KOi K00602.
OMAi AGDKANC.
OrthoDBi EOG74N5GD.
PhylomeDBi O35567.
TreeFami TF105642.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
Reactomei REACT_217264. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

NextBioi 615152.
PROi O35567.

Gene expression databases

Genevestigatori O35567.

Family and domain databases

Gene3Di 1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
InterProi IPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 95 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

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