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Database: UniProt
Entry: A0A2G8T521_9BURK
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ID   A0A2G8T521_9BURK        Unreviewed;       356 AA.
AC   A0A2G8T521;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000256|ARBA:ARBA00014401};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
DE            EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404};
DE   AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000256|ARBA:ARBA00031520};
DE   AltName: Full=p-protein {ECO:0000256|ARBA:ARBA00031175};
GN   ORFNames=CR103_03290 {ECO:0000313|EMBL:PIL41141.1};
OS   Massilia psychrophila.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1603353 {ECO:0000313|EMBL:PIL41141.1, ECO:0000313|Proteomes:UP000228593};
RN   [1] {ECO:0000313|EMBL:PIL41141.1, ECO:0000313|Proteomes:UP000228593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 30813 {ECO:0000313|EMBL:PIL41141.1,
RC   ECO:0000313|Proteomes:UP000228593};
RA   Wang H.;
RT   "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT   isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate and the decarboxylation/dehydration of prephenate to
CC       phenylpyruvate. {ECO:0000256|ARBA:ARBA00002364}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC         Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC         Evidence={ECO:0000256|ARBA:ARBA00000913};
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:0000256|ARBA:ARBA00000824};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004741}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC       prephenate from chorismate: step 1/1. {ECO:0000256|ARBA:ARBA00004817}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIL41141.1}.
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DR   EMBL; PDOB01000003; PIL41141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8T521; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000228593; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04905; ACT_CM-PDT; 1.
DR   CDD; cd13630; PBP2_PDT_1; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   NCBIfam; TIGR01807; CM_P2; 1.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF48600; Chorismate mutase II; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000228593}.
FT   DOMAIN          1..89
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          89..264
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          276..353
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            257
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   356 AA;  38496 MW;  26348CF3E417F06B CRC64;
     MTDKLTPLRE QIDAIDAELL DLLNQRARLA QQVGHVKAET RAPVFRPERE AQVLRGVAAR
     NPGPLKNADL QTIFREVMSA CRSLEKRVTV AYLGPAGTFS EQAVYQQFGG AVDGLPCVSI
     DEVFRATEAG TADFGVVPVE NSSEGAINRT LDLMLATTTI ISGEVSIPVH HSLMSSTGSM
     DGVTVVCAHS QALAQCQVWL NQHYPNIERR AVASNAEAAV MASTNPAIAA IASEMAGEQY
     KLGVVQGHIQ DDPHNRTRFA IIGHLQTNPS GEDQTSLVLA VPNKAGAVYN LLAPLAKHGV
     SMTRFESRPA RIGTWEYYFY VDIEGHVFDA AVARALEELK DNAAFFKVLG SYPLSL
//
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