AROH_THETH
ID AROH_THETH Reviewed; 122 AA.
AC Q84FH6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Chorismate mutase AroH;
DE EC=5.4.99.5 {ECO:0000269|PubMed:14727008};
GN Name=aroH {ECO:0000250|UniProtKB:P19080};
GN Synonyms=aroG {ECO:0000303|PubMed:14727008};
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CHORISMATE MUTASE,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=HB27;
RX PubMed=14727008; DOI=10.1007/s00203-003-0639-z;
RA Helmstaedt K., Heinrich G., Merkl R., Braus G.H.;
RT "Chorismate mutase of Thermus thermophilus is a monofunctional AroH class
RT enzyme inhibited by tyrosine.";
RL Arch. Microbiol. 181:195-203(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS), AND SUBUNIT.
RC STRAIN=HB8;
RA Inagaki E., Kuramitsu S., Yokoyama S., Miyano M., Tahirov T.H.;
RT "The crystal structure of chorismate mutase from Thermus Thermophilus.";
RL Submitted (JUN-2003) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate. Probably involved in the aromatic amino acid biosynthesis.
CC {ECO:0000269|PubMed:14727008}.
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:14727008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898;
CC Evidence={ECO:0000269|PubMed:14727008};
CC -!- ACTIVITY REGULATION: Inhibited by 40% with 500 uM tyrosine, and a
CC tyrosine concentration as high as 5 mM reduced activity to 5%.
CC {ECO:0000269|PubMed:14727008}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=290 uM for chorismate (at pH 7.6 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:14727008};
CC Vmax=198 umol/min/mg enzyme (at pH 7.6 and at 70 degrees Celsius)
CC {ECO:0000269|PubMed:14727008};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:14727008};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:14727008, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; AY196198; AAO40746.1; -; Genomic_DNA.
DR RefSeq; WP_011172959.1; NZ_VHHQ01000003.1.
DR PDB; 1ODE; X-ray; 1.65 A; A/B/C=1-122.
DR PDB; 1UFY; X-ray; 0.96 A; A=1-122.
DR PDB; 1UI9; X-ray; 1.65 A; A=1-122.
DR PDBsum; 1ODE; -.
DR PDBsum; 1UFY; -.
DR PDBsum; 1UI9; -.
DR AlphaFoldDB; Q84FH6; -.
DR SMR; Q84FH6; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB02201; Malonate Ion.
DR GeneID; 3169087; -.
DR OMA; CIRVMMT; -.
DR BRENDA; 5.4.99.5; 2305.
DR UniPathway; UPA00120; UER00203.
DR EvolutionaryTrace; Q84FH6; -.
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; Isomerase.
FT CHAIN 1..122
FT /note="Chorismate mutase AroH"
FT /id="PRO_0000414908"
FT DOMAIN 2..120
FT /note="Chorismate mutase aroH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00514"
FT BINDING 6
FT /ligand="prephenate"
FT /ligand_id="ChEBI:CHEBI:29934"
FT /evidence="ECO:0000250|UniProtKB:P19080"
FT BINDING 89
FT /ligand="prephenate"
FT /ligand_id="ChEBI:CHEBI:29934"
FT /evidence="ECO:0000250|UniProtKB:P19080"
FT BINDING 107
FT /ligand="prephenate"
FT /ligand_id="ChEBI:CHEBI:29934"
FT /evidence="ECO:0000250|UniProtKB:P19080"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1UFY"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1UFY"
FT HELIX 16..33
FT /evidence="ECO:0007829|PDB:1UFY"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1UFY"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:1UFY"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:1UFY"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1UFY"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1UFY"
FT STRAND 85..95
FT /evidence="ECO:0007829|PDB:1UFY"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1UFY"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1UFY"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:1UFY"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1UFY"
SQ SEQUENCE 122 AA; 13650 MW; 76BE0A500B3EE4E3 CRC64;
MVRGIRGAIT VEEDTPEAIH QATRELLLKM LEANGIQSYE ELAAVIFTVT EDLTSAFPAE
AARQIGMHRV PLLSAREVPV PGSLPRVIRV LALWNTDTPQ DRVRHVYLRE AVRLRPDLES
AQ
