ID A0A923HL66_9BURK Unreviewed; 357 AA. AC A0A923HL66; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 03-MAY-2023, entry version 2. 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:MBC3862894.1}; GN ORFNames=H8K32_12350 {ECO:0000313|EMBL:MBC3862894.1}; OS Undibacterium jejuense. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Undibacterium. OX NCBI_TaxID=1344949 {ECO:0000313|EMBL:MBC3862894.1, ECO:0000313|Proteomes:UP000634011}; RN [1] {ECO:0000313|EMBL:MBC3862894.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KACC 12607 {ECO:0000313|EMBL:MBC3862894.1}; RA Lu H.; RT "Novel species isolated from subtropical streams in China."; RL Submitted (AUG-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:MBC3862894.1}. 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; JACOFV010000011; MBC3862894.1; -; Genomic_DNA. DR Proteomes; UP000634011; Unassembled WGS sequence. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. 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 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; 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:MBC3862894.1}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}. FT DOMAIN 1..90 FT /note="Chorismate mutase" FT /evidence="ECO:0000259|PROSITE:PS51168" FT DOMAIN 90..265 FT /note="Prephenate dehydratase" FT /evidence="ECO:0000259|PROSITE:PS51171" FT DOMAIN 277..354 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" SQ SEQUENCE 357 AA; 38871 MW; A9CE6E2B28D94762 CRC64; MSDNKLLPLR QKIDAIDAQI LDLLNQRARV AEEVGHVKAE TNAPVFRPER EAQVLRSVAE RNPGPLLSDD IQLIFREIMS ACRALERRVV VAFLGPVGTF SEQAVYKQFG HAIQALPCVS IDEVFRATEA GTADFGVVPI ENSSEGAINR TLDLLLQTSL IISGELAIPV QHSLMGKSGN MEGVSRICAH SQALAQCQAW LNQHYPHIER HAVASNAEAA RMASGDFTVA AIASEIAGQQ YNLGIVSAHI QDDPHNRTRF AVVGRLQTTP SGKDQTSIVL ATPNKAGAVY NLLAPLSKHG VSMTRFESRP ARTGNWEYYF YVDVEGHVQD TKVAAAMADL NDKAAFFKVL GSYPCTL //