CHMU_EMENI
ID CHMU_EMENI Reviewed; 267 AA.
AC G5EB37; A0A1U8QN24; C8V2P3; Q5AXW4; Q9Y7B2;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Chorismate mutase {ECO:0000303|PubMed:10428795};
DE Short=CM {ECO:0000305};
DE EC=5.4.99.5 {ECO:0000269|PubMed:10428795};
DE AltName: Full=AnCM {ECO:0000303|PubMed:10428795};
GN Name=aroC {ECO:0000303|PubMed:10428795};
GN ORFNames=ANIA_06866 {ECO:0000312|EMBL:CBF71622.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000312|Proteomes:UP000000560};
RN [1] {ECO:0000312|EMBL:AAD30065.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, INDUCTION, AND
RP MUTAGENESIS OF ASP-233.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000303|PubMed:10428795};
RX PubMed=10428795; DOI=10.1074/jbc.274.32.22275;
RA Krappmann S., Helmstaedt K., Gerstberger T., Eckert S., Hoffmann B.,
RA Hoppert M., Schnappauf G., Braus G.H.;
RT "The aroC gene of Aspergillus nidulans codes for a monofunctional,
RT allosterically regulated chorismate mutase.";
RL J. Biol. Chem. 274:22275-22282(1999).
RN [2] {ECO:0000312|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000312|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3] {ECO:0000312|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000312|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate (PubMed:10428795). Acts at the first branch point in the
CC aromatic amino acid pathway where it steers biosynthesis towards
CC phenylalanine and tyrosine, and away from tryptophan (By similarity).
CC {ECO:0000250|UniProtKB:P32178, ECO:0000269|PubMed:10428795}.
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:10428795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000269|PubMed:10428795};
CC -!- ACTIVITY REGULATION: Each dimer has two allosteric binding sites that
CC can bind the regulatory effectors tryptophan or tyrosine
CC (PubMed:10428795). Can bind either one tryptophan or one tyrosine, two
CC tryptophan or two tyrosine or one tryptophan and one tyrosine, which
CC differentially affect the catalytic activity (By similarity). Activated
CC by tryptophan and subject to feedback inhibition by tyrosine
CC (PubMed:10428795). In the presence of both tryptophan and tyrosine, the
CC enzyme is in the activated state (By similarity).
CC {ECO:0000250|UniProtKB:P32178, ECO:0000269|PubMed:10428795}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for chorismate (in the presence of 5 uM tryptophan and at
CC 30 degrees Celsius);
CC Note=kcat is 82 sec(-1) with chorismate as substrate (at 30 degrees
CC Celsius). kcat is 92 sec(-1) with chorismate as substrate (in the
CC presence of 5 uM tryptophan and at 30 degrees Celsius). kcat is 82.5
CC sec(-1) with chorismate as substrate (in the presence of 50 uM
CC tyrosine at 30 degrees Celsius). {ECO:0000269|PubMed:10428795};
CC pH dependence:
CC Optimum pH is 5.9 in the absence of effectors. Optimum pH is 7.1 in
CC the presence of tryptophan. Optimum pH is 5.4 in the presence of
CC tyrosine. Tryptophan broadens the pH range of detectable catalytic
CC activity. {ECO:0000269|PubMed:10428795};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:10428795}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10428795}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32178}.
CC -!- INDUCTION: Not induced by histidine starvation.
CC {ECO:0000269|PubMed:10428795}.
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DR EMBL; AF133241; AAD30065.1; -; Genomic_DNA.
DR EMBL; AACD01000113; EAA58265.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF71622.1; -; Genomic_DNA.
DR RefSeq; XP_664470.1; XM_659378.1.
DR AlphaFoldDB; G5EB37; -.
DR SMR; G5EB37; -.
DR STRING; 162425.CADANIAP00007666; -.
DR EnsemblFungi; CBF71622; CBF71622; ANIA_06866.
DR EnsemblFungi; EAA58265; EAA58265; AN6866.2.
DR GeneID; 2870568; -.
DR KEGG; ani:AN6866.2; -.
DR VEuPathDB; FungiDB:AN6866; -.
DR eggNOG; KOG0795; Eukaryota.
DR HOGENOM; CLU_057757_0_0_1; -.
DR InParanoid; G5EB37; -.
DR OMA; DVNCLQA; -.
DR OrthoDB; 1087630at2759; -.
DR BRENDA; 5.4.99.5; 517.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:AspGD.
DR GO; GO:0120284; F:tryptophan binding; IEA:EnsemblFungi.
DR GO; GO:0072545; F:tyrosine binding; IEA:EnsemblFungi.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IMP:AspGD.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; ISO:UniProtKB.
DR GO; GO:0000909; P:sporocarp development involved in sexual reproduction; IMP:AspGD.
DR GO; GO:0006571; P:tyrosine biosynthetic process; ISO:UniProtKB.
DR Gene3D; 1.10.590.10; -; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR008238; Chorismate_mutase_AroQ_euk.
DR InterPro; IPR037039; CM_AroQ_sf_eucaryotic.
DR PANTHER; PTHR21145; PTHR21145; 1.
DR PIRSF; PIRSF017318; Chor_mut_AroQ_eu; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01802; CM_pl-yst; 1.
DR PROSITE; PS51169; CHORISMATE_MUT_3; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Cytoplasm; Isomerase;
KW Phenylalanine biosynthesis; Reference proteome; Tyrosine biosynthesis.
FT CHAIN 1..267
FT /note="Chorismate mutase"
FT /id="PRO_0000452012"
FT DOMAIN 7..262
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT BINDING 77
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 78
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 145
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 145
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 147
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 147
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 148
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 148
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 151
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT MUTAGEN 233
FT /note="D->I,T: Decreases activity regulation by tyrosine
FT and tryptophan."
FT /evidence="ECO:0000269|PubMed:10428795"
SQ SEQUENCE 267 AA; 30661 MW; 72FB25CAB2291593 CRC64;
MDTAIDLSDA SKALDLANIR FQLIRLEDTI TFHLIERVQF PLNKTIYIPG GVKIPNEQIS
LMDYLLRETE RLQSRVRRYQ SPDEYPFFPS ALEKPILQPL DYPKILHDND VNVNETIKTR
YVQDILPAIC PQFGGREDRG ETQENYGSAA TCDVSCLQAL SRRIHFGKFV AESKFQKETE
KFVALIKAGD RKEIDEAITD AKVEQKVLER LALKAKTYGT DPGFPEQSGP KIDVQAVQDM
YKEYVIPLTK VVEVEYLMQR LKGTQWE
