CHMU_PICAN
ID CHMU_PICAN Reviewed; 280 AA.
AC Q9P4D8;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Chorismate mutase {ECO:0000303|PubMed:10894726};
DE Short=CM {ECO:0000305};
DE EC=5.4.99.5 {ECO:0000269|PubMed:10894726};
GN Name=ARO7 {ECO:0000305}; Synonyms=HARO7 {ECO:0000303|PubMed:10894726};
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730 {ECO:0000312|EMBL:AAF87954.1};
RN [1] {ECO:0000312|EMBL:AAF87954.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, AND INDUCTION.
RC STRAIN=RB11 {ECO:0000303|PubMed:10894726};
RX PubMed=10894726; DOI=10.1128/jb.182.15.4188-4197.2000;
RA Krappmann S., Pries R., Gellissen G., Hiller M., Braus G.H.;
RT "HARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula
RT polymorpha and is derepressed upon methanol utilization.";
RL J. Bacteriol. 182:4188-4197(2000).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate (PubMed:10894726). 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 (PubMed:10894726).
CC {ECO:0000269|PubMed:10894726}.
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:10894726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000269|PubMed:10894726};
CC -!- ACTIVITY REGULATION: Each dimer has two allosteric binding sites that
CC can bind the regulatory effectors tryptophan or tyrosine
CC (PubMed:10894726). 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:10894726). 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:10894726}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for chorismate (in the presence of 10 uM tryptophan and at
CC 37 degrees Celsius) {ECO:0000269|PubMed:10894726};
CC Note=kcat is 303.8 sec(-1) with chorismate as substrate (in the
CC presence of 10 uM tryptophan and at 37 degrees Celsius). kcat is 89.3
CC sec(-1) with chorismate as substrate (in the presence of 100 uM
CC tyrosine and at 37 degrees Celsius). {ECO:0000269|PubMed:10894726};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius.
CC {ECO:0000269|PubMed:10894726};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:10894726}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10894726}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32178}.
CC -!- INDUCTION: Induced by growth on methanol carbon source
CC (PubMed:10894726). Slightly induced by growth on the non-fermentable
CC carbon source glycerol (PubMed:10894726). Not induced by histidine
CC starvation (PubMed:10894726). {ECO:0000269|PubMed:10894726}.
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; AF204738; AAF87954.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P4D8; -.
DR SMR; Q9P4D8; -.
DR PhylomeDB; Q9P4D8; -.
DR BRENDA; 5.4.99.5; 2587.
DR UniPathway; UPA00120; UER00203.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IMP: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; Tyrosine biosynthesis.
FT CHAIN 1..280
FT /note="Chorismate mutase"
FT /id="PRO_0000452013"
FT DOMAIN 3..256
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00516"
FT BINDING 73
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
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 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"
FT BINDING 139
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 139
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 140
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
FT BINDING 140
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /ligand_note="allosteric effector"
FT /evidence="ECO:0000250|UniProtKB:P32178"
SQ SEQUENCE 280 AA; 32069 MW; 689D49312CD292D9 CRC64;
MDFMKPETVL DLGNIRDALV RMEDTIIFNF IERSQFYASP SVYKVNQFPI PNFDGSFLDW
LLSQHERIHS QVRRYDAPDE VPFFPNVLEK TFLPKINYPS VLASYADEIN VNKEILKIYT
SEIVPGIAAG SGEQEDNLGS CAMADIECLQ SLSRRIHFGR FVAEAKFISE GDKIVDLIKK
RDVEGIEALI TNAEVEKRIL DRLLEKGRAY GTDPTLKFTQ HIQSKVKPEV IVKIYKDFVI
PLTKKVEVDY LLRRLEDEED DDATQKSGGY VDRFLSSGLY
