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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

    Pathway:iprephenate 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), 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei7 – 71Substrate
    Binding sitei90 – 901Substrate

    GO - Molecular functioni

    • chorismate mutase activity Source: UniProtKB

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: UniProtKB-KW
    • chorismate metabolic process Source: UniProtKB
    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
    ProteomesiUP000001570 Componenti: Chromosome

    Organism-specific databases

    GenoListiBSU22690. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781E → A: No chorismate mutase activity. 1 Publication
    Mutagenesisi90 – 901R → A: No chorismate mutase activity. 1 Publication
    Mutagenesisi90 – 901R → G: 2-fold decrease in affinity and very low decrease in catalytic efficiency. 1 Publication
    Mutagenesisi90 – 901R → K: Low decrease in catalytic efficiency and in affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 127127Chorismate mutase AroHPRO_0000119203Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.3 Publications

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100012466.

    Structurei

    Secondary structure

    1
    127
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1110Combined sources
    Beta strandi13 – 153Combined sources
    Helixi17 – 3519Combined sources
    Helixi39 – 413Combined sources
    Beta strandi42 – 498Combined sources
    Helixi59 – 635Combined sources
    Beta strandi65 – 673Combined sources
    Beta strandi73 – 775Combined sources
    Beta strandi86 – 9712Combined sources
    Helixi101 – 1033Combined sources
    Helixi110 – 1156Combined sources
    Helixi121 – 1244Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-127.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19080.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 121119Chorismate mutase aroH-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 7832Substrate bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000043606.
    InParanoidiP19080.
    KOiK06208.
    OMAiCIRVMMT.
    OrthoDBiEOG6WT8J3.
    PhylomeDBiP19080.

    Family and domain databases

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti112 – 1121V → A in AAA22249 (PubMed:2105742).Curated

    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
    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. Positions 1-127.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100012466.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    GenoListiBSU22690. [Micado]

    Phylogenomic databases

    HOGENOMiHOG000043606.
    InParanoidiP19080.
    KOiK06208.
    OMAiCIRVMMT.
    OrthoDBiEOG6WT8J3.
    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

    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli."
      Gray J.V., Golinelli-Pimpaneau B., Knowles J.R.
      Biochemistry 29:376-383(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-35, FUNCTION AS A CHORISMATE MUTASE, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
    2. "Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR, aro(B,E,F,H), trp(A-F), hisH, and tyrA genes."
      Henner D.J.
      Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "Mutagenesis study of active site residues in chorismate mutase from Bacillus subtilis."
      Cload S.T., Liu D.R., Pastor R.M., Schultz P.G.
      J. Am. Chem. Soc. 118:1787-1788(1996)
      Cited for: MUTAGENESIS, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Electrostatic catalysis of the Claisen rearrangement: probing the role of Glu78 in Bacillus subtilis chorismate mutase by genetic selection."
      Kast P., Hartgerink J.D., Asif-Ullah M., Hilvert D.
      J. Am. Chem. Soc. 118:3069-3070(1996)
      Cited for: MUTAGENESIS OF GLU-78.
    6. "13C NMR studies of the enzyme-product complex of Bacillus subtilis chorismate mutase."
      Rajagopalan J.S., Taylor K.M., Jaffe E.K.
      Biochemistry 32:3965-3972(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    7. "Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog."
      Chook Y.M., Ke H., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 90:8600-8603(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.
    8. "The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction."
      Chook Y.M., Gray J.V., Ke H., Lipscomb W.N.
      J. Mol. Biol. 240:476-500(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
    9. "The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase catalytic homotrimer."
      Ladner J.E., Reddy P., Davis A., Tordova M., Howard A.J., Gilliland G.L.
      Acta Crystallogr. D 56:673-683(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), SUBUNIT.
    10. "A strategically positioned cation is crucial for efficient catalysis by chorismate mutase."
      Kast P., Grisostomi C., Chen I.A., Li S., Krengel U., Xue Y., Hilvert D.
      J. Biol. Chem. 275:36832-36838(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT SER-88/LYS-90 AND LYS-88/SER-90, MUTAGENESIS OF ARG-90, BIOPHYSICOCHEMICAL PROPERTIES.

    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: June 24, 2015
    This is version 127 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

    External Data

    Dasty 3

    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 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.