CHMU_SCHPO
ID CHMU_SCHPO Reviewed; 251 AA.
AC O13739;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chorismate mutase;
DE Short=CM;
DE EC=5.4.99.5 {ECO:0000250|UniProtKB:P32178};
GN Name=aro7 {ECO:0000312|PomBase:SPAC16E8.04c}; ORFNames=SPAC16E8.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate (By similarity). 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}.
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:0000250|UniProtKB:P32178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000250|UniProtKB:P32178};
CC -!- ACTIVITY REGULATION: Each dimer has two allosteric binding sites that
CC can bind the regulatory effectors tryptophan or tyrosine (By
CC similarity). 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 (By
CC similarity). In the presence of both tryptophan and tyrosine, the
CC enzyme is in the activated state (By similarity).
CC {ECO:0000250|UniProtKB:P32178}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P32178}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P32178}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32178}.
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DR EMBL; CU329670; CAB11033.1; -; Genomic_DNA.
DR PIR; T37784; T37784.
DR RefSeq; NP_594216.1; NM_001019639.2.
DR AlphaFoldDB; O13739; -.
DR SMR; O13739; -.
DR STRING; 4896.SPAC16E8.04c.1; -.
DR iPTMnet; O13739; -.
DR MaxQB; O13739; -.
DR PaxDb; O13739; -.
DR PRIDE; O13739; -.
DR EnsemblFungi; SPAC16E8.04c.1; SPAC16E8.04c.1:pep; SPAC16E8.04c.
DR GeneID; 2542334; -.
DR KEGG; spo:SPAC16E8.04c; -.
DR PomBase; SPAC16E8.04c; -.
DR VEuPathDB; FungiDB:SPAC16E8.04c; -.
DR eggNOG; KOG0795; Eukaryota.
DR HOGENOM; CLU_057757_0_0_1; -.
DR InParanoid; O13739; -.
DR OMA; FLDWALM; -.
DR PhylomeDB; O13739; -.
DR UniPathway; UPA00120; UER00203.
DR PRO; PR:O13739; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004106; F:chorismate mutase activity; ISS:PomBase.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; ISS:PomBase.
DR GO; GO:0006568; P:tryptophan metabolic process; NAS:PomBase.
DR GO; GO:0006571; P:tyrosine biosynthetic process; ISS:PomBase.
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 3: Inferred from homology;
KW Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Cytoplasm; Isomerase;
KW Phenylalanine biosynthesis; Reference proteome; Tyrosine biosynthesis.
FT CHAIN 1..251
FT /note="Chorismate mutase"
FT /id="PRO_0000119205"
FT DOMAIN 1..251
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT BINDING 74
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 75
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 134
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 134
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 136
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 136
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 137
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 137
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
SQ SEQUENCE 251 AA; 29050 MW; 1AC18AE4C1E6C4B7 CRC64;
MSLVNEKLKL ENIRSALIRQ EDTIIFNFLE RAQFPRNEKV YKSGKEGCLN LENYDGSFLN
YLLHEEEKVY ALVRRYASPE EYPFTDNLPE PILPKFSGKF PLHPNNVNVN SEILEYYINE
IVPKISSPGD DFDNYGSTVV CDIRCLQSLS RRIHYGKFVA EAKYLANPEK YKKLILARDI
KGIENEIVDA AQEERVLKRL HYKALNYGRD AADPTKPSDR INADCVASIY KDYVIPMTKK
VEVDYLLARL L
