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P31335

- PUR9_CHICK

UniProt

P31335 - PUR9_CHICK

Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei138 – 1381Proton acceptorSequence Analysis
    Sitei267 – 2671Transition state stabilizerSequence Analysis
    Active sitei268 – 2681Proton acceptorCurated
    Binding sitei317 – 3171AICAR; via carbonyl oxygen1 Publication
    Binding sitei340 – 3401AICAR1 Publication
    Binding sitei432 – 4321AICAR; shared with dimeric partnerBy similarity
    Binding sitei452 – 4521AICAR; shared with dimeric partnerBy similarity
    Binding sitei542 – 5421AICAR; via carbonyl oxygen; shared with dimeric partnerBy similarity
    Binding sitei589 – 5891AICAR; shared with dimeric partner1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 153IMP
    Nucleotide bindingi35 – 384IMP
    Nucleotide bindingi65 – 684IMP
    Nucleotide bindingi102 – 1054IMP
    Nucleotide bindingi126 – 1283IMP

    GO - Molecular functioni

    1. IMP cyclohydrolase activity Source: Reactome
    2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: Reactome
    3. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: Reactome
    2. nucleobase-containing small molecule metabolic process Source: Reactome
    3. purine nucleobase metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_116007. De novo synthesis of IMP.
    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
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 593593Bifunctional purine biosynthesis protein PURHPRO_0000192155Add
    BLAST

    Proteomic databases

    PaxDbiP31335.
    PRIDEiP31335.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    593
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 137
    Helixi18 – 2710
    Beta strandi31 – 344
    Helixi36 – 449
    Beta strandi49 – 513
    Helixi52 – 565
    Helixi62 – 643
    Beta strandi66 – 683
    Helixi71 – 788
    Helixi83 – 919
    Beta strandi97 – 1037
    Helixi107 – 1115
    Beta strandi113 – 1153
    Helixi118 – 1225
    Helixi128 – 13811
    Turni139 – 1424
    Beta strandi144 – 1463
    Helixi149 – 1513
    Helixi152 – 1609
    Helixi169 – 19830
    Turni201 – 2033
    Beta strandi204 – 2085
    Beta strandi210 – 2123
    Beta strandi218 – 2214
    Beta strandi223 – 2264
    Beta strandi228 – 2347
    Helixi238 – 25821
    Beta strandi262 – 2676
    Beta strandi270 – 2767
    Helixi282 – 2876
    Turni291 – 2933
    Helixi294 – 2963
    Helixi299 – 30911
    Turni312 – 3176
    Beta strandi318 – 3247
    Helixi328 – 3358
    Beta strandi339 – 3457
    Helixi349 – 3579
    Helixi358 – 3614
    Beta strandi364 – 3685
    Beta strandi376 – 3827
    Beta strandi385 – 3906
    Helixi398 – 4014
    Beta strandi406 – 4083
    Helixi413 – 42715
    Beta strandi429 – 4324
    Beta strandi434 – 4385
    Beta strandi441 – 4466
    Helixi452 – 46817
    Helixi472 – 4754
    Helixi485 – 49713
    Helixi504 – 5107
    Beta strandi513 – 5153
    Helixi522 – 5298
    Beta strandi535 – 5417
    Helixi547 – 5537
    Turni554 – 5563
    Beta strandi557 – 5637
    Helixi569 – 57911
    Beta strandi582 – 5876

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G8MX-ray1.75A/B1-593[»]
    1M9NX-ray1.93A/B1-593[»]
    1OZ0X-ray2.50A/B1-593[»]
    1THZX-ray1.80A/B1-593[»]
    2B1GX-ray2.10A/B/C/D1-593[»]
    2B1IX-ray2.02A/B1-593[»]
    2IU0X-ray2.53A/B1-593[»]
    2IU3X-ray2.90A/B1-593[»]
    ProteinModelPortaliP31335.
    SMRiP31335. Positions 4-593.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31335.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni208 – 2092AICAR binding

    Domaini

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

    Sequence similaritiesi

    Belongs to the PurH family.Curated

    Phylogenomic databases

    eggNOGiCOG0138.
    HOGENOMiHOG000230372.
    HOVERGENiHBG006912.
    InParanoidiP31335.
    KOiK00602.
    PhylomeDBiP31335.

    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.

    P31335-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAARQQLALL SVSEKAGLVE FARSLNALGL GLIASGGTAT ALRDAGLPVR    50
    DVSDLTGFPE MLGGRVKTLH PAVHAGILAR NIPEDNADMN KQDFSLVRVV 100
    VCNLYPFVKT VSSPGVTVPE AVEKIDIGGV ALLRAAAKNH ARVTVVCDPA 150
    DYSSVAKEMA ASKDKDTSVE TRRHLALKAF THTAQYDAAI SDYFRKEYSK 200
    GVSQLPLRYG MNPHQSPAQL YTTRPKLPLT VVNGSPGFIN LCDALNAWQL 250
    VKELKQALGI PAAASFKHVS PAGAAVGIPL SEEEAQVCMV HDLHKTLTPL 300
    ASAYARSRGA DRMSSFGDFI ALSDICDVPT AKIISREVSD GVVAPGYEEE 350
    ALKILSKKKN GGYCVLQMDP NYEPDDNEIR TLYGLQLMQK RNNAVIDRSL 400
    FKNIVTKNKT LPESAVRDLI VASIAVKYTQ SNSVCYAKDG QVIGIGAGQQ 450
    SRIHCTRLAG DKANSWWLRH HPRVLSMKFK AGVKRAEVSN AIDQYVTGTI 500
    GEDEDLVKWQ AMFEEVPAQL TEAEKKQWIA KLTAVSLSSD AFFPFRDNVD 550
    RAKRIGVQFI VAPSGSAADE VVIEACNELG ITLIHTNLRL FHH 593
    Length:593
    Mass (Da):64,415
    Last modified:July 1, 1993 - v1
    Checksum:iBD1A34F03D96A136
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S64492 mRNA. Translation: AAB20309.1.
    PIRiJQ1281. DTCHPH.
    RefSeqiNP_990509.1. NM_205178.1.
    UniGeneiGga.4556.

    Genome annotation databases

    GeneIDi396091.
    KEGGigga:396091.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S64492 mRNA. Translation: AAB20309.1 .
    PIRi JQ1281. DTCHPH.
    RefSeqi NP_990509.1. NM_205178.1.
    UniGenei Gga.4556.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G8M X-ray 1.75 A/B 1-593 [» ]
    1M9N X-ray 1.93 A/B 1-593 [» ]
    1OZ0 X-ray 2.50 A/B 1-593 [» ]
    1THZ X-ray 1.80 A/B 1-593 [» ]
    2B1G X-ray 2.10 A/B/C/D 1-593 [» ]
    2B1I X-ray 2.02 A/B 1-593 [» ]
    2IU0 X-ray 2.53 A/B 1-593 [» ]
    2IU3 X-ray 2.90 A/B 1-593 [» ]
    ProteinModelPortali P31335.
    SMRi P31335. Positions 4-593.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P31335.
    PRIDEi P31335.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396091.
    KEGGi gga:396091.

    Organism-specific databases

    CTDi 471.

    Phylogenomic databases

    eggNOGi COG0138.
    HOGENOMi HOG000230372.
    HOVERGENi HBG006912.
    InParanoidi P31335.
    KOi K00602.
    PhylomeDBi P31335.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00133 .
    UPA00074 ; UER00135 .
    Reactomei REACT_116007. De novo synthesis of IMP.

    Miscellaneous databases

    EvolutionaryTracei P31335.
    NextBioi 20816149.
    PROi P31335.

    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. "De novo purine nucleotide biosynthesis: cloning, sequencing and expression of a chicken PurH cDNA encoding 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase-IMP cyclohydrolase."
      Ni L., Guan K., Zalkin H., Dixon J.E.
      Gene 106:197-205(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis."
      Greasley S.E., Horton P., Ramcharan J., Beardsley G.P., Benkovic S.J., Wilson I.A.
      Nat. Struct. Biol. 8:402-406(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GMP, SUBUNIT.
    3. "Structural insights into the avian AICAR transformylase mechanism."
      Wolan D.W., Greasley S.E., Beardsley G.P., Wilson I.A.
      Biochemistry 41:15505-15513(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH AICAR AND XMP, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiPUR9_CHICK
    AccessioniPrimary (citable) accession number: P31335
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 97 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

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3