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P19080

- AROH_BACSU

UniProt

P19080 - AROH_BACSU

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Protein
Chorismate mutase AroH
Gene
aroH, BSU22690
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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, 1 Publication)3 Publications
  2. KM=87 µM for chorismate (at pH 7.5 and at 30 degrees Celsius)
  3. KM=100 µM for chorismate (at pH 7.5 and at 30 degrees Celsius, 1 Publication)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei7 – 71Substrate
Binding sitei90 – 901Substrate

GO - Molecular functioni

  1. chorismate mutase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-KW
  2. 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. 700.
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: Chromosome

Organism-specific databases

GenoListiBSU22690. [Micado]

Subcellular locationi

Cytoplasm Reviewed prediction

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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 AroH
PRO_0000119203Add
BLAST

Interactioni

Subunit structurei

Homotrimer.3 Publications

Protein-protein interaction databases

STRINGi224308.BSU22690.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP19080.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 121119Chorismate mutase aroH-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 7832Substrate binding By similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000043606.
KOiK06208.
OMAiGWTYVPV.
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

MMIRGIRGAT TVERDTEEEI LQKTKQLLEK IIEENHTKPE DVVQMLLSAT    50
PDLHAVFPAK AVRELSGWQY VPVTCMQEMD VTGGLKKCIR VMMTVQTDVP 100
QDQIRHVYLE KVVVLRPDLS LTKNTEL 127
Length:127
Mass (Da):14,517
Last modified:October 19, 2002 - v2
Checksum:i5A803614FE1F402E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121V → A in AAA22249. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M32278 Genomic DNA. Translation: AAA22249.1 .
M80245 Genomic DNA. Translation: AAA20861.1 .
AL009126 Genomic DNA. Translation: CAB14185.1 .
PIRi A33894.
RefSeqi NP_390150.1. NC_000964.3.
WP_009967606.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1COM X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 1-127 [» ]
1DBF X-ray 1.30 A/B/C 1-127 [» ]
1FNJ X-ray 1.90 A 1-127 [» ]
1FNK X-ray 2.00 A 1-127 [» ]
2CHS X-ray 1.90 A/B/C/D/E/F/G/H/I/J/K/L 1-127 [» ]
2CHT X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 1-127 [» ]
3ZO8 X-ray 1.59 A/B/C/D/E/F 1-127 [» ]
3ZOP X-ray 1.61 A/B/C/D/E/F 1-127 [» ]
3ZP4 X-ray 1.80 A/B/C/D/E/F 1-127 [» ]
3ZP7 X-ray 1.70 A/B/C/D/E/F 1-127 [» ]
ProteinModelPortali P19080.
SMRi P19080. Positions 1-127.
ModBasei Search...

Protein-protein interaction databases

STRINGi 224308.BSU22690.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14185 ; CAB14185 ; BSU22690 .
GeneIDi 939005.
KEGGi bsu:BSU22690.
PATRICi 18976347. VBIBacSub10457_2364.

Organism-specific databases

GenoListi BSU22690. [Micado ]

Phylogenomic databases

HOGENOMi HOG000043606.
KOi K06208.
OMAi GWTYVPV.
OrthoDBi EOG6WT8J3.
PhylomeDBi P19080.

Enzyme and pathway databases

UniPathwayi UPA00120 ; UER00203 .
BioCyci BSUB:BSU22690-MONOMER.
BRENDAi 5.4.99.5. 700.
SABIO-RK P19080.

Miscellaneous databases

EvolutionaryTracei P19080.

Family and domain databases

Gene3Di 3.30.1330.40. 1 hit.
InterProi IPR008243. Chorismate_mutase_AroH.
IPR013813. Endoribo_LPSP/chorism_mut-like.
[Graphical view ]
PANTHERi PTHR21164. PTHR21164. 1 hit.
Pfami PF07736. CM_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF005965. Chor_mut_AroH. 1 hit.
ProDomi PD031888. Chorismate_mutase_AroH. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF55298. SSF55298. 1 hit.
TIGRFAMsi TIGR01796. CM_mono_aroH. 1 hit.
PROSITEi PS51167. CHORISMATE_MUT_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 119 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

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