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Protein

Chorismate mutase AroH

Gene

aroH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.1 Publication

Catalytic activityi

Chorismate = prephenate.

Kineticsi

  1. KM=67 µM for chorismate (at pH 7.5 and at 30 degrees Celsius, PubMed:10960481)3 Publications
  2. KM=87 µM for chorismate (at pH 7.5 and at 30 degrees Celsius)3 Publications
  3. KM=100 µM for chorismate (at pH 7.5 and at 30 degrees Celsius, PubMed:2105742)3 Publications

    Pathwayi: prephenate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Chorismate mutase AroH (aroH), Chorismate mutase AroH (aroH), Protein AroA(G) (aroA)
    This subpathway is part of the pathway prephenate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes prephenate from chorismate, the pathway prephenate biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei7Substrate1
    Binding sitei90Substrate1

    GO - Molecular functioni

    • chorismate mutase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Enzyme and pathway databases

    BioCyciBSUB:BSU22690-MONOMER.
    BRENDAi5.4.99.5. 658.
    SABIO-RKP19080.
    UniPathwayiUPA00120; UER00203.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chorismate mutase AroH (EC:5.4.99.5)
    Short name:
    CM
    Gene namesi
    Name:aroH
    Ordered Locus Names:BSU22690
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi78E → A: No chorismate mutase activity. 1 Publication1
    Mutagenesisi90R → A: No chorismate mutase activity. 1 Publication1
    Mutagenesisi90R → G: 2-fold decrease in affinity and very low decrease in catalytic efficiency. 1 Publication1
    Mutagenesisi90R → K: Low decrease in catalytic efficiency and in affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001192031 – 127Chorismate mutase AroHAdd BLAST127

    Proteomic databases

    PaxDbiP19080.
    PRIDEiP19080.

    Interactioni

    Subunit structurei

    Homotrimer.3 Publications

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100012466.

    Structurei

    Secondary structure

    1127
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 11Combined sources10
    Beta strandi13 – 15Combined sources3
    Helixi17 – 35Combined sources19
    Helixi39 – 41Combined sources3
    Beta strandi42 – 49Combined sources8
    Helixi59 – 63Combined sources5
    Beta strandi65 – 67Combined sources3
    Beta strandi73 – 77Combined sources5
    Beta strandi86 – 97Combined sources12
    Helixi101 – 103Combined sources3
    Helixi110 – 115Combined sources6
    Helixi121 – 124Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1COMX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
    1DBFX-ray1.30A/B/C1-127[»]
    1FNJX-ray1.90A1-127[»]
    1FNKX-ray2.00A1-127[»]
    2CHSX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
    2CHTX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
    3ZO8X-ray1.59A/B/C/D/E/F1-127[»]
    3ZOPX-ray1.61A/B/C/D/E/F1-127[»]
    3ZP4X-ray1.80A/B/C/D/E/F1-127[»]
    3ZP7X-ray1.70A/B/C/D/E/F1-127[»]
    ProteinModelPortaliP19080.
    SMRiP19080.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19080.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini3 – 121Chorismate mutase aroH-typePROSITE-ProRule annotationAdd BLAST119

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni47 – 78Substrate bindingBy similarityAdd BLAST32

    Sequence similaritiesi

    Contains 1 chorismate mutase aroH-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4105KHN. Bacteria.
    COG4401. LUCA.
    HOGENOMiHOG000043606.
    InParanoidiP19080.
    KOiK06208.
    OMAiCIRVMMT.
    PhylomeDBiP19080.

    Family and domain databases

    CDDicd02185. AroH. 1 hit.
    Gene3Di3.30.1330.40. 1 hit.
    InterProiIPR008243. Chorismate_mutase_AroH.
    IPR013813. Endoribo_LPSP/chorism_mut-like.
    [Graphical view]
    PANTHERiPTHR21164. PTHR21164. 1 hit.
    PfamiPF07736. CM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005965. Chor_mut_AroH. 1 hit.
    ProDomiPD031888. Chorismate_mutase_AroH. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF55298. SSF55298. 1 hit.
    TIGRFAMsiTIGR01796. CM_mono_aroH. 1 hit.
    PROSITEiPS51167. CHORISMATE_MUT_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19080-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMIRGIRGAT TVERDTEEEI LQKTKQLLEK IIEENHTKPE DVVQMLLSAT
    60 70 80 90 100
    PDLHAVFPAK AVRELSGWQY VPVTCMQEMD VTGGLKKCIR VMMTVQTDVP
    110 120
    QDQIRHVYLE KVVVLRPDLS LTKNTEL
    Length:127
    Mass (Da):14,517
    Last modified:October 19, 2002 - v2
    Checksum:i5A803614FE1F402E
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti112V → A in AAA22249 (PubMed:2105742).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32278 Genomic DNA. Translation: AAA22249.1.
    M80245 Genomic DNA. Translation: AAA20861.1.
    AL009126 Genomic DNA. Translation: CAB14185.1.
    PIRiA33894.
    RefSeqiNP_390150.1. NC_000964.3.
    WP_009967606.1. NZ_JNCM01000036.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14185; CAB14185; BSU22690.
    GeneIDi939005.
    KEGGibsu:BSU22690.
    PATRICi18976347. VBIBacSub10457_2364.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32278 Genomic DNA. Translation: AAA22249.1.
    M80245 Genomic DNA. Translation: AAA20861.1.
    AL009126 Genomic DNA. Translation: CAB14185.1.
    PIRiA33894.
    RefSeqiNP_390150.1. NC_000964.3.
    WP_009967606.1. NZ_JNCM01000036.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1COMX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
    1DBFX-ray1.30A/B/C1-127[»]
    1FNJX-ray1.90A1-127[»]
    1FNKX-ray2.00A1-127[»]
    2CHSX-ray1.90A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
    2CHTX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-127[»]
    3ZO8X-ray1.59A/B/C/D/E/F1-127[»]
    3ZOPX-ray1.61A/B/C/D/E/F1-127[»]
    3ZP4X-ray1.80A/B/C/D/E/F1-127[»]
    3ZP7X-ray1.70A/B/C/D/E/F1-127[»]
    ProteinModelPortaliP19080.
    SMRiP19080.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100012466.

    Proteomic databases

    PaxDbiP19080.
    PRIDEiP19080.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB14185; CAB14185; BSU22690.
    GeneIDi939005.
    KEGGibsu:BSU22690.
    PATRICi18976347. VBIBacSub10457_2364.

    Phylogenomic databases

    eggNOGiENOG4105KHN. Bacteria.
    COG4401. LUCA.
    HOGENOMiHOG000043606.
    InParanoidiP19080.
    KOiK06208.
    OMAiCIRVMMT.
    PhylomeDBiP19080.

    Enzyme and pathway databases

    UniPathwayiUPA00120; UER00203.
    BioCyciBSUB:BSU22690-MONOMER.
    BRENDAi5.4.99.5. 658.
    SABIO-RKP19080.

    Miscellaneous databases

    EvolutionaryTraceiP19080.
    PROiP19080.

    Family and domain databases

    CDDicd02185. AroH. 1 hit.
    Gene3Di3.30.1330.40. 1 hit.
    InterProiIPR008243. Chorismate_mutase_AroH.
    IPR013813. Endoribo_LPSP/chorism_mut-like.
    [Graphical view]
    PANTHERiPTHR21164. PTHR21164. 1 hit.
    PfamiPF07736. CM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005965. Chor_mut_AroH. 1 hit.
    ProDomiPD031888. Chorismate_mutase_AroH. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF55298. SSF55298. 1 hit.
    TIGRFAMsiTIGR01796. CM_mono_aroH. 1 hit.
    PROSITEiPS51167. CHORISMATE_MUT_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAROH_BACSU
    AccessioniPrimary (citable) accession number: P19080
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: October 19, 2002
    Last modified: November 30, 2016
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This enzyme is monofunctional, and its activity is unaffected by the end-product aromatic amino acids.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.