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Q5R5C2

- PUR9_PONAB

UniProt

Q5R5C2 - PUR9_PONAB

Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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: UniProtKB-EC
    2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-EC
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 592592Bifunctional purine biosynthesis protein PURHPRO_0000270213Add
    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

    PRIDEiQ5R5C2.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R5C2.
    SMRiQ5R5C2. 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

    HOVERGENiHBG006912.
    KOiK00602.

    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.

    Q5R5C2-1 [UniParc]FASTAAdd to Basket

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    MAPGHLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD    50
    VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA 100
    CNLYPFVKTV ASPGVTVEEA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED 150
    YVVVSTEMKS SEIKDTSLET RRQLALKAFT HTAQYDEAIS DYFRKQYSKG 200
    ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL CDALNAWQLV 250
    KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS 300
    AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA 350
    LKILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF 400
    SNVVTKNKDL PESALRDLIV ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS 450
    RIHCTRLAGD KANYWWLRHH PQVLSMKFKT GVKRAEISNA IDQYVTGTIG 500
    EDEDLIKWEA LFEEVPELLT EAEKKEWVEK LTEVSISSDA FFPFRDNVDR 550
    AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH 592
    Length:592
    Mass (Da):64,693
    Last modified:December 21, 2004 - v1
    Checksum:i4991DDFCCD8D0E7B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860940 mRNA. Translation: CAH93044.1.
    RefSeqiNP_001126800.1. NM_001133328.1.

    Genome annotation databases

    GeneIDi100173804.
    KEGGipon:100173804.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860940 mRNA. Translation: CAH93044.1 .
    RefSeqi NP_001126800.1. NM_001133328.1.

    3D structure databases

    ProteinModelPortali Q5R5C2.
    SMRi Q5R5C2. Positions 4-592.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5R5C2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100173804.
    KEGGi pon:100173804.

    Organism-specific databases

    CTDi 471.

    Phylogenomic databases

    HOVERGENi HBG006912.
    KOi K00602.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiPUR9_PONAB
    AccessioniPrimary (citable) accession number: Q5R5C2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 58 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