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Protein

Phosphoribosyl-AMP cyclohydrolase

Gene

hisI

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.UniRule annotation1 Publication

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.UniRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication
  • Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Kineticsi

kcat is 8 sec(-1).

  1. KM=14 µM for phosphoribosyl-AMP1 Publication

    Pathwayi: L-histidine biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
    Proteins known to be involved in the 9 steps of the subpathway in this organism are:
    1. ATP phosphoribosyltransferase (hisG)
    2. Phosphoribosyl-ATP pyrophosphatase (hisE)
    3. Phosphoribosyl-AMP cyclohydrolase (hisI)
    4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
    5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
    6. Imidazoleglycerol-phosphate dehydratase (hisB)
    7. Histidinol-phosphate aminotransferase (hisC)
    8. no protein annotated in this organism
    9. Histidinol dehydrogenase (hisD)
    This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi85 – 851MagnesiumCurated
    Metal bindingi86 – 861Zinc; shared with dimeric partnerCurated
    Metal bindingi87 – 871MagnesiumCurated
    Metal bindingi89 – 891MagnesiumCurated
    Metal bindingi102 – 1021Zinc; shared with dimeric partnerCurated
    Metal bindingi109 – 1091Zinc; shared with dimeric partnerCurated

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMTHE187420:GJNM-245-MONOMER.
    UniPathwayiUPA00031; UER00008.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosyl-AMP cyclohydrolaseUniRule annotation (EC:3.5.4.19UniRule annotation)
    Short name:
    PRA-CHUniRule annotation
    Gene namesi
    Name:hisIUniRule annotation
    Ordered Locus Names:MTH_245
    OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
    Taxonomic identifieri187420 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
    Proteomesi
    • UP000005223 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 138138Phosphoribosyl-AMP cyclohydrolasePRO_0000136511Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi187420.MTH245.

    Structurei

    Secondary structure

    1
    138
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73Combined sources
    Helixi9 – 113Combined sources
    Beta strandi18 – 203Combined sources
    Beta strandi24 – 307Combined sources
    Turni31 – 333Combined sources
    Beta strandi36 – 427Combined sources
    Helixi44 – 5310Combined sources
    Beta strandi57 – 604Combined sources
    Turni61 – 644Combined sources
    Beta strandi65 – 684Combined sources
    Turni69 – 735Combined sources
    Beta strandi77 – 848Combined sources
    Beta strandi88 – 9912Combined sources
    Beta strandi105 – 1095Combined sources
    Beta strandi112 – 1154Combined sources
    Beta strandi118 – 1214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZPSX-ray1.70A/B1-138[»]
    ProteinModelPortaliO26347.
    SMRiO26347. Positions 4-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO26347.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PRA-CH family.UniRule annotation

    Phylogenomic databases

    eggNOGiarCOG02676. Archaea.
    COG0139. LUCA.
    KOiK01496.
    OMAiGPACHTN.

    Family and domain databases

    HAMAPiMF_01021. HisI.
    InterProiIPR026660. PRA-CH.
    IPR002496. PRib_AMP_CycHydrolase_dom.
    [Graphical view]
    PfamiPF01502. PRA-CH. 1 hit.
    [Graphical view]
    ProDomiPD002610. PRA_CycHdrlase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequencei

    Sequence statusi: Complete.

    O26347-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIKSKGDVNI LLNFRHNING EDLIIAVAQD HETGEVLMVA YMNREALRRT
    60 70 80 90 100
    LETGTAHYWS TSRGKLWLKG ESSGHVQRVK DVLVDCDGDA VVLKVEQEGG
    110 120 130
    ACHTGYRSCF YRSIDGDELK VREDAVKVFD PEEIYGDG
    Length:138
    Mass (Da):15,458
    Last modified:January 1, 1998 - v1
    Checksum:iABE62FDD2235C067
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000666 Genomic DNA. Translation: AAB84751.1.
    PIRiF69130.

    Genome annotation databases

    EnsemblBacteriaiAAB84751; AAB84751; MTH_245.
    KEGGimth:MTH_245.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000666 Genomic DNA. Translation: AAB84751.1.
    PIRiF69130.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZPSX-ray1.70A/B1-138[»]
    ProteinModelPortaliO26347.
    SMRiO26347. Positions 4-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi187420.MTH245.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAB84751; AAB84751; MTH_245.
    KEGGimth:MTH_245.

    Phylogenomic databases

    eggNOGiarCOG02676. Archaea.
    COG0139. LUCA.
    KOiK01496.
    OMAiGPACHTN.

    Enzyme and pathway databases

    UniPathwayiUPA00031; UER00008.
    BioCyciMTHE187420:GJNM-245-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiO26347.

    Family and domain databases

    HAMAPiMF_01021. HisI.
    InterProiIPR026660. PRA-CH.
    IPR002496. PRib_AMP_CycHydrolase_dom.
    [Graphical view]
    PfamiPF01502. PRA-CH. 1 hit.
    [Graphical view]
    ProDomiPD002610. PRA_CycHdrlase. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
    2. "Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI."
      Sivaraman J., Myers R.S., Boju L., Sulea T., Cygler M., Jo Davisson V., Schrag J.D.
      Biochemistry 44:10071-10080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH CADMIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, METAL-BINDING SITES.

    Entry informationi

    Entry nameiHIS3_METTH
    AccessioniPrimary (citable) accession number: O26347
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 1, 1998
    Last modified: July 6, 2016
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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

    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 one 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.