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O35567

- PUR9_RAT

UniProt

O35567 - PUR9_RAT

Protein

Bifunctional purine biosynthesis protein PURH

Gene

Atic

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      Previous versions | rss
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    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

    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

    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.
    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.
    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

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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

    Experimental Info

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

    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.
    HAMAPi MF_00139. PurH.
    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

    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: October 1, 2014
    This is version 96 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