CHMU_PSEAE
ID CHMU_PSEAE Reviewed; 185 AA.
AC Q9HU05; G3XCM9; Q7BCC7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Monofunctional chorismate mutase {ECO:0000250|UniProtKB:P42517, ECO:0000312|EMBL:AAK73353.1};
DE EC=5.4.99.5 {ECO:0000269|PubMed:11532214};
DE Flags: Precursor;
GN Name=aroQ {ECO:0000303|PubMed:11532214}; OrderedLocusNames=PA5184;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK73353.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-33, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000312|EMBL:AAK73353.1};
RX PubMed=11532214; DOI=10.1186/gb-2001-2-8-research0030;
RA Calhoun D.H., Bonner C.A., Gu W., Xie G., Jensen R.A.;
RT "The emerging periplasm-localized subclass of AroQ chorismate mutases,
RT exemplified by those from Salmonella typhimurium and Pseudomonas
RT aeruginosa.";
RL Genome Biol. 2:RESEARCH0030.1-RESEARCH0030.16(2001).
RN [2] {ECO:0000312|EMBL:AAG08569.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate. The joint presence of this enzyme together with
CC cyclohexadienyl dehydratase and aromatic aminotransferase in the
CC periplasmic compartment comprises a complete three-step chorismate to
CC phenylalanine pathway and accounts for the so called hidden overflow
CC pathway to phenylalanine in P.aeruginosa, in which two possible routes
CC for it exists, namely either via phenylpyruvate or L-arogenate.
CC {ECO:0000250|UniProtKB:P0A9J8, ECO:0000269|PubMed:11532214}.
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:11532214};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=98 uM for chorismate (at 32 degrees Celsius)
CC {ECO:0000269|PubMed:11532214};
CC Note=kcat is 6.4 sec(-1) for chorismate.
CC {ECO:0000269|PubMed:11532214};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000250|UniProtKB:P42517}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11532214}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11532214}.
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DR EMBL; AE004091; AAG08569.1; -; Genomic_DNA.
DR EMBL; AF389865; AAK73353.1; -; Genomic_DNA.
DR PIR; D82998; D82998.
DR RefSeq; NP_253871.1; NC_002516.2.
DR RefSeq; WP_003114063.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HU05; -.
DR SMR; Q9HU05; -.
DR STRING; 287.DR97_2554; -.
DR PaxDb; Q9HU05; -.
DR PRIDE; Q9HU05; -.
DR DNASU; 881600; -.
DR EnsemblBacteria; AAG08569; AAG08569; PA5184.
DR GeneID; 881600; -.
DR KEGG; pae:PA5184; -.
DR PATRIC; fig|208964.12.peg.5433; -.
DR PseudoCAP; PA5184; -.
DR HOGENOM; CLU_090313_2_1_6; -.
DR InParanoid; Q9HU05; -.
DR OMA; RSAPDCP; -.
DR PhylomeDB; Q9HU05; -.
DR BioCyc; PAER208964:G1FZ6-5303-MON; -.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0004106; F:chorismate mutase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic 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; IPR008240; Chorismate_mutase_periplasmic.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR Pfam; PF01817; CM_2; 1.
DR PIRSF; PIRSF026640; Peripl_chor_mut; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48600; SSF48600; 1.
DR TIGRFAMs; TIGR01806; CM_mono2; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Isomerase; Periplasm;
KW Phenylalanine biosynthesis; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:11532214"
FT CHAIN 24..185
FT /note="Monofunctional chorismate mutase"
FT /evidence="ECO:0000269|PubMed:11532214"
FT /id="PRO_0000419448"
FT DOMAIN 24..104
FT /note="Chorismate mutase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00515,
FT ECO:0000305"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J8"
SQ SEQUENCE 185 AA; 20417 MW; F9B6CF52DFD488C9 CRC64;
MRPSFASWGL LALLLLQGPL LQAQPLSPAL QQLLSLSSQR LQLADQVAQS KAQSGKAVQD
SPREEQQLQM LAGQAGSHGV GAEQVRLLFA AQIEANKLVQ YRLLSRPLPD AGQAVDLERI
RSRLNQLNLE LLRGYAPALA ELRVDDCRPR LNQALQRQVR VDRLDELHAI ALSRAAGDLC
HWAEL
