AROH_BACSU
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 03-AUG-2022, entry version 158.
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; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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 / NCIMB
RC 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.
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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; NZ_JNCM01000036.1.
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 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; -.
DR AlphaFoldDB; P19080; -.
DR BMRB; P19080; -.
DR SMR; P19080; -.
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; P19080; -.
DR PRIDE; P19080; -.
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 OMA; CIRVMMT; -.
DR PhylomeDB; P19080; -.
DR BioCyc; BSUB:BSU22690-MON; -.
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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR CDD; cd02185; AroH; 1.
DR Gene3D; 3.30.1330.40; -; 1.
DR InterPro; IPR008243; Chorismate_mutase_AroH.
DR InterPro; IPR035959; RutC-like_sf.
DR PANTHER; PTHR21164; PTHR21164; 1.
DR Pfam; PF07736; CM_1; 1.
DR PIRSF; PIRSF005965; Chor_mut_AroH; 1.
DR SUPFAM; SSF55298; SSF55298; 1.
DR TIGRFAMs; TIGR01796; CM_mono_aroH; 1.
DR PROSITE; PS51167; CHORISMATE_MUT_1; 1.
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
