ID E6KWD8_9PAST Unreviewed; 387 AA. AC E6KWD8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 24-JAN-2024, entry version 47. 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:EFU67819.1}; GN ORFNames=HMPREF9064_0482 {ECO:0000313|EMBL:EFU67819.1}; OS Aggregatibacter segnis ATCC 33393. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Aggregatibacter. OX NCBI_TaxID=888057 {ECO:0000313|EMBL:EFU67819.1, ECO:0000313|Proteomes:UP000032871}; RN [1] {ECO:0000313|EMBL:EFU67819.1, ECO:0000313|Proteomes:UP000032871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33393 {ECO:0000313|EMBL:EFU67819.1, RC ECO:0000313|Proteomes:UP000032871}; RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G., RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A., RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., RA Petrosino J., Highlander S., Gibbs R.; RL Submitted (DEC-2010) 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:EFU67819.1}. 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; AEPS01000003; EFU67819.1; -; Genomic_DNA. DR RefSeq; WP_006717331.1; NZ_LS483443.1. DR AlphaFoldDB; E6KWD8; -. DR STRING; 739.GCA_001059425_00899; -. DR GeneID; 60799883; -. DR HOGENOM; CLU_035008_1_0_6; -. DR OrthoDB; 9802281at2; -. DR UniPathway; UPA00120; UER00203. DR UniPathway; UPA00121; UER00345. DR Proteomes; UP000032871; 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; cd13631; PBP2_Ct-PDT_like; 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; IPR010952; CM_P_1. DR InterPro; IPR001086; Preph_deHydtase. DR InterPro; IPR018528; Preph_deHydtase_CS. DR NCBIfam; TIGR01797; CM_P_1; 1. DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1. DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 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; PS00857; PREPHENATE_DEHYDR_1; 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, ECO:0000313|EMBL:EFU67819.1}; 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:UP000032871}. FT DOMAIN 1..92 FT /note="Chorismate mutase" FT /evidence="ECO:0000259|PROSITE:PS51168" FT DOMAIN 105..285 FT /note="Prephenate dehydratase" FT /evidence="ECO:0000259|PROSITE:PS51171" FT DOMAIN 299..376 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT BINDING 9 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1" FT BINDING 26 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1" FT BINDING 37 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1" FT BINDING 46 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1" FT BINDING 50 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1" FT BINDING 84 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1" FT BINDING 88 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-1" FT SITE 278 FT /note="Essential for prephenate dehydratase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2" SQ SEQUENCE 387 AA; 44178 MW; 27D6A1AE0325BCF1 CRC64; MSLDLSEIRQ QITQIDRSLL KLLSERHRLA FDVVRSKELT QKPLRDAERE EQLLQELVQF AENENYQLEP QYITSIFQKI IEDSVLTQQV YLQKKLNAQR EQNIHIAFLG KRGSYSHLAA RNYATRYQEE LVEISCASFD EVFAKVQHGE ADYGVLPLEN TTSGAINEVY DLLQHTDLFL VGELAYPIQH CVLVNGQDDL SKIDTLYSHP QVIQQCSHFI HGLERVHIEY CESSSHAMQL VAGLNKPNIA ALGNEDGGKL YGLNVLKRNV ANQENNITRF IVIAKKPHSV SPQIHTKTLL LMSTGQQAGA LVDALLVFKK HHINMTKLES RPIYGKPWEE MFYLEIEANI HHPDTQSALE ELKQFSHYLK ILGCYPSEIV KPTALPK //