CHMU_METJA
ID CHMU_METJA Reviewed; 99 AA.
AC Q57696;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Chorismate mutase;
DE Short=CM;
DE EC=5.4.99.5;
DE AltName: Full=Monofunctional chorismate mutase AroQ(f);
GN Name=aroQ; Synonyms=aroQ(f); OrderedLocusNames=MJ0246;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=9665711; DOI=10.1021/bi980449t;
RA MacBeath G., Kast P., Hilvert D.;
RT "A small, thermostable, and monofunctional chorismate mutase from the
RT archaeon Methanococcus jannaschii.";
RL Biochemistry 37:10062-10073(1998).
RN [3]
RP STRUCTURE BY NMR OF 1-93.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=17994104; DOI=10.1038/nsmb1325;
RA Pervushin K., Vamvaca K., Vogeli B., Hilvert D.;
RT "Structure and dynamics of a molten globular enzyme.";
RL Nat. Struct. Mol. Biol. 14:1202-1206(2007).
CC -!- FUNCTION: Catalyzes the conversion of chorismate into prephenate via a
CC Claisen rearrangement. {ECO:0000269|PubMed:9665711}.
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:9665711};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41 uM for chorismate (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:9665711};
CC Note=kcat is 5.7 sec(-1) (at 30 degrees Celsius).;
CC pH dependence:
CC Activity is independent of pH in the range of pH 5-9.
CC {ECO:0000269|PubMed:9665711};
CC Temperature dependence:
CC Thermostable. The midpoint for its thermal unfolding transition (Tm)
CC is 88 degrees Celsius. {ECO:0000269|PubMed:9665711};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9665711}.
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DR EMBL; L77117; AAB98234.1; -; Genomic_DNA.
DR PIR; G64330; G64330.
DR PDB; 2GTV; NMR; -; X=1-93.
DR PDBsum; 2GTV; -.
DR AlphaFoldDB; Q57696; -.
DR SMR; Q57696; -.
DR STRING; 243232.MJ_0246; -.
DR EnsemblBacteria; AAB98234; AAB98234; MJ_0246.
DR KEGG; mja:MJ_0246; -.
DR eggNOG; arCOG02098; Archaea.
DR HOGENOM; CLU_131518_4_0_2; -.
DR InParanoid; Q57696; -.
DR OMA; MDYNKEV; -.
DR PhylomeDB; Q57696; -.
DR SABIO-RK; Q57696; -.
DR UniPathway; UPA00120; UER00203.
DR EvolutionaryTrace; Q57696; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.20.59.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR010950; Chorismate_mutase_arc.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR Pfam; PF01817; CM_2; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01791; CM_archaeal; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..99
FT /note="Chorismate mutase"
FT /id="PRO_0000119202"
FT DOMAIN 1..90
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:2GTV"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:2GTV"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:2GTV"
FT HELIX 69..93
FT /evidence="ECO:0007829|PDB:2GTV"
SQ SEQUENCE 99 AA; 11782 MW; 9759018D0A07E76C CRC64;
MIEKLAEIRK KIDEIDNKIL KLIAERNSLA KDVAEIKNQL GIPINDPERE KYIYDRIRKL
CKEHNVDENI GIKIFQILIE HNKALQKQYL EETQNKNKK
