ID A0A845G3Y8_9BURK Unreviewed; 357 AA. AC A0A845G3Y8; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 14-DEC-2022, entry version 5. 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 Name=pheA {ECO:0000313|EMBL:MYM88350.1}; GN ORFNames=GTP91_14345 {ECO:0000313|EMBL:MYM88350.1}; OS Duganella vulcania. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Massilia group; Duganella. OX NCBI_TaxID=2692166 {ECO:0000313|EMBL:MYM88350.1, ECO:0000313|Proteomes:UP000470302}; RN [1] {ECO:0000313|EMBL:MYM88350.1, ECO:0000313|Proteomes:UP000470302} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FT82W {ECO:0000313|EMBL:MYM88350.1, RC ECO:0000313|Proteomes:UP000470302}; RA Lu H.; RT "Novel species isolated from a subtropical stream in China."; RL Submitted (JAN-2020) 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:MYM88350.1}. 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; WWCW01000044; MYM88350.1; -; Genomic_DNA. DR AlphaFoldDB; A0A845G3Y8; -. DR UniPathway; UPA00120; UER00203. DR UniPathway; UPA00121; UER00345. DR Proteomes; UP000470302; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro. DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.59.10; -; 1. 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 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 TIGRFAMs; TIGR01807; CM_P2; 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, ECO:0000313|EMBL:MYM88350.1}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}. 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 357 AA; 38758 MW; 13580BA47067699E CRC64; MTDKLTPLRE QIDAIDAQIL DLLNQRAKVA QQVGHVKAET NAPVFRPERE AQVLRGVAER NPGPMGDVEL QTIWREIMSA CRSLEKRVTI AFLGPAGTYT EQAAYQQFGT AVDVLPCSSI DEVFRATEAG TAEFGVVPVE NSTEGAIGRT LDLLLHTSLS ISGEVSLAVR HSLLSGTGNM DGVTAICAHA QALAQCQIWL NNNYPDIERR AVSSNAEAAR MARDDHTIAA IAGERAGVRY GLGTVKANIQ DDPHNRTRFA VIGQLQAGRS GQDRTSLALA APHKAGSIYR LLGSLARHNV SMTRFESRPA RTGTWEYYFY VDVEGHVQDE GVAKALEELQ SNAAFFKVLG SYPVSLN //