ID AROH_BACSU Reviewed; 127 AA. AC P19080; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 2. DT 02-SEP-2026, entry version 170. DE RecName: Full=Chorismate mutase AroH; DE Short=CM; DE EC=5.4.99.5 {ECO:0000269|PubMed:2105742}; GN Name=aroH {ECO:0000303|PubMed:2105742}; OrderedLocusNames=BSU22690; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-35, FUNCTION AS A RP CHORISMATE MUTASE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / RC NCIMB 3610 / NRRL NRS-744 / VKM B-501; RX PubMed=2105742; DOI=10.1021/bi00454a011; RA Gray J.V., Golinelli-Pimpaneau B., Knowles J.R.; RT "Monofunctional chorismate mutase from Bacillus subtilis: purification of RT the protein, molecular cloning of the gene, and overexpression of the gene RT product in Escherichia coli."; RL Biochemistry 29:376-383(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Henner D.J.; RT "Sequence of Bacillus subtilis dbpA, mtr(A,B), gerC(1-3), ndk, cheR, RT aro(B,E,F,H), trp(A-F), hisH, and tyrA genes."; RL Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP MUTAGENESIS, AND BIOPHYSICOCHEMICAL PROPERTIES. RX DOI=10.1021/ja953152g; RA Cload S.T., Liu D.R., Pastor R.M., Schultz P.G.; RT "Mutagenesis study of active site residues in chorismate mutase from RT Bacillus subtilis."; RL J. Am. Chem. Soc. 118:1787-1788(1996). RN [5] RP MUTAGENESIS OF GLU-78. RX DOI=10.1021/ja953701i; RA Kast P., Hartgerink J.D., Asif-Ullah M., Hilvert D.; RT "Electrostatic catalysis of the Claisen rearrangement: probing the role of RT Glu78 in Bacillus subtilis chorismate mutase by genetic selection."; RL J. Am. Chem. Soc. 118:3069-3070(1996). RN [6] RP STRUCTURE BY NMR. RX PubMed=8471608; DOI=10.1021/bi00066a017; RA Rajagopalan J.S., Taylor K.M., Jaffe E.K.; RT "13C NMR studies of the enzyme-product complex of Bacillus subtilis RT chorismate mutase."; RL Biochemistry 32:3965-3972(1993). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT. RX PubMed=8378335; DOI=10.1073/pnas.90.18.8600; RA Chook Y.M., Ke H., Lipscomb W.N.; RT "Crystal structures of the monofunctional chorismate mutase from Bacillus RT subtilis and its complex with a transition state analog."; RL Proc. Natl. Acad. Sci. U.S.A. 90:8600-8603(1993). RN [8] {ECO:0007744|PDB:1COM} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PREPHENATE, AND RP SUBUNIT. RX PubMed=8046752; DOI=10.1006/jmbi.1994.1462; RA Chook Y.M., Gray J.V., Ke H., Lipscomb W.N.; RT "The monofunctional chorismate mutase from Bacillus subtilis. Structure RT determination of chorismate mutase and its complexes with a transition RT state analog and prephenate, and implications for the mechanism of the RT enzymatic reaction."; RL J. Mol. Biol. 240:476-500(1994). RN [9] {ECO:0007744|PDB:1DBF} RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), AND SUBUNIT. RX PubMed=10818343; DOI=10.1107/s0907444900004625; RA Ladner J.E., Reddy P., Davis A., Tordova M., Howard A.J., Gilliland G.L.; RT "The 1.30 A resolution structure of the Bacillus subtilis chorismate mutase RT catalytic homotrimer."; RL Acta Crystallogr. D 56:673-683(2000). RN [10] {ECO:0007744|PDB:1FNJ, ECO:0007744|PDB:1FNK} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT SER-88/LYS-90 AND RP LYS-88/SER-90, MUTAGENESIS OF ARG-90, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10960481; DOI=10.1074/jbc.m006351200; RA Kast P., Grisostomi C., Chen I.A., Li S., Krengel U., Xue Y., Hilvert D.; RT "A strategically positioned cation is crucial for efficient catalysis by RT chorismate mutase."; RL J. Biol. Chem. 275:36832-36838(2000). CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to CC prephenate. Probably involved in the aromatic amino acid biosynthesis. CC {ECO:0000269|PubMed:2105742}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; CC Evidence={ECO:0000269|PubMed:2105742}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; CC Evidence={ECO:0000269|PubMed:2105742}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=67 uM for chorismate (at pH 7.5 and at 30 degrees Celsius) CC {ECO:0000269|PubMed:10960481}; CC KM=87 uM for chorismate (at pH 7.5 and at 30 degrees Celsius) CC {ECO:0000269|Ref.4}; CC KM=100 uM for chorismate (at pH 7.5 and at 30 degrees Celsius) CC {ECO:0000269|PubMed:2105742}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; CC prephenate from chorismate: step 1/1. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10818343, CC ECO:0000269|PubMed:8046752, ECO:0000269|PubMed:8378335}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- MISCELLANEOUS: This enzyme is monofunctional, and its activity is CC unaffected by the end-product aromatic amino acids. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M32278; AAA22249.1; -; Genomic_DNA. DR EMBL; M80245; AAA20861.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14185.1; -; Genomic_DNA. DR PIR; A33894; A33894. DR RefSeq; NP_390150.1; NC_000964.3. DR RefSeq; WP_009967606.1; NC_000964.3. DR PDB; 1COM; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-127. DR PDB; 1DBF; X-ray; 1.30 A; A/B/C=1-127. DR PDB; 1FNJ; X-ray; 1.90 A; A=1-127. DR PDB; 1FNK; X-ray; 2.00 A; A=1-127. DR PDB; 2CHS; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-127. DR PDB; 2CHT; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-127. DR PDB; 3ZO8; X-ray; 1.59 A; A/B/C/D/E/F=1-127. DR PDB; 3ZOP; X-ray; 1.61 A; A/B/C/D/E/F=1-127. DR PDB; 3ZP4; X-ray; 1.80 A; A/B/C/D/E/F=1-127. DR PDB; 3ZP7; X-ray; 1.70 A; A/B/C/D/E/F=1-127. DR AlphaFoldDB; P19080; -. DR BMRB; P19080; -. DR SMR; P19080; -. DR FunCoup; P19080; 122. DR STRING; 224308.BSU22690; -. DR DrugBank; DB02153; 3-sulfino-L-alanine. DR DrugBank; DB08648; 8-Hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid. DR DrugBank; DB08427; Prephenic acid. DR PaxDb; 224308-BSU22690; -. DR EnsemblBacteria; CAB14185; CAB14185; BSU_22690. DR GeneID; 939005; -. DR KEGG; bsu:BSU22690; -. DR PATRIC; fig|224308.179.peg.2473; -. DR eggNOG; COG4401; Bacteria. DR InParanoid; P19080; -. DR OrthoDB; 9802232at2; -. DR PhylomeDB; P19080; -. DR BioCyc; BSUB:BSU22690-MONOMER; -. DR BRENDA; 5.4.99.5; 658. DR SABIO-RK; P19080; -. DR UniPathway; UPA00120; UER00203. DR EvolutionaryTrace; P19080; -. DR PRO; PR:P19080; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB. DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB. DR CDD; cd02185; AroH; 1. DR Gene3D; 3.30.1330.40; RutC-like; 1. DR InterPro; IPR008243; Chorismate_mutase_AroH. DR InterPro; IPR035959; RutC-like_sf. DR NCBIfam; TIGR01796; CM_mono_aroH; 1. DR PANTHER; PTHR21164; CHORISMATE MUTASE; 1. DR PANTHER; PTHR21164:SF0; CHORISMATE MUTASE AROH; 1. DR Pfam; PF07736; CM_1; 1. DR PIRSF; PIRSF005965; Chor_mut_AroH; 1. DR SUPFAM; SSF55298; YjgF-like; 1. DR PROSITE; PS51167; CHORISMATE_MUT_1; 1. DR PDBsum; 1COM; -. DR PDBsum; 1DBF; -. DR PDBsum; 1FNJ; -. DR PDBsum; 1FNK; -. DR PDBsum; 2CHS; -. DR PDBsum; 2CHT; -. DR PDBsum; 3ZO8; -. DR PDBsum; 3ZOP; -. DR PDBsum; 3ZP4; -. DR PDBsum; 3ZP7; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Cytoplasm; Direct protein sequencing; Isomerase; Reference proteome. FT CHAIN 1..127 FT /note="Chorismate mutase AroH" FT /id="PRO_0000119203" FT DOMAIN 3..121 FT /note="Chorismate mutase aroH-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00514" FT BINDING 7 FT /ligand="prephenate" FT /ligand_id="ChEBI:CHEBI:29934" FT /evidence="ECO:0000269|PubMed:8046752, FT ECO:0007744|PDB:1COM" FT BINDING 74..78 FT /ligand="prephenate" FT /ligand_id="ChEBI:CHEBI:29934" FT /evidence="ECO:0000269|PubMed:8046752, FT ECO:0007744|PDB:1COM" FT BINDING 90 FT /ligand="prephenate" FT /ligand_id="ChEBI:CHEBI:29934" FT /evidence="ECO:0000269|PubMed:8046752, FT ECO:0007744|PDB:1COM" FT BINDING 108 FT /ligand="prephenate" FT /ligand_id="ChEBI:CHEBI:29934" FT /evidence="ECO:0000269|PubMed:8046752, FT ECO:0007744|PDB:1COM" FT MUTAGEN 78 FT /note="E->A: No chorismate mutase activity." FT /evidence="ECO:0000269|Ref.5" FT MUTAGEN 90 FT /note="R->A: No chorismate mutase activity." FT /evidence="ECO:0000269|PubMed:10960481" FT MUTAGEN 90 FT /note="R->G: 2-fold decrease in affinity and very low FT decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:10960481" FT MUTAGEN 90 FT /note="R->K: Low decrease in catalytic efficiency and in FT affinity." FT /evidence="ECO:0000269|PubMed:10960481" FT CONFLICT 112 FT /note="V -> A (in Ref. 1; AAA22249)" FT /evidence="ECO:0000305" FT STRAND 2..11 FT /evidence="ECO:0007829|PDB:1DBF" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:2CHS" FT HELIX 17..35 FT /evidence="ECO:0007829|PDB:1DBF" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1DBF" FT STRAND 42..49 FT /evidence="ECO:0007829|PDB:1DBF" FT HELIX 59..63 FT /evidence="ECO:0007829|PDB:1DBF" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:1FNJ" FT STRAND 73..77 FT /evidence="ECO:0007829|PDB:1DBF" FT STRAND 86..97 FT /evidence="ECO:0007829|PDB:1DBF" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:1DBF" FT HELIX 110..115 FT /evidence="ECO:0007829|PDB:1DBF" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:1DBF" SQ SEQUENCE 127 AA; 14517 MW; 5A803614FE1F402E CRC64; MMIRGIRGAT TVERDTEEEI LQKTKQLLEK IIEENHTKPE DVVQMLLSAT PDLHAVFPAK AVRELSGWQY VPVTCMQEMD VTGGLKKCIR VMMTVQTDVP QDQIRHVYLE KVVVLRPDLS LTKNTEL //