ID PHEA_CORGL Reviewed; 315 AA. AC P10341; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2002, sequence version 2. DT 04-NOV-2026, entry version 147. DE RecName: Full=Prephenate dehydratase; DE Short=PDT; DE EC=4.2.1.51; GN Name=pheA; OrderedLocusNames=Cgl2899, cg3207; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC OS 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / OS 534). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3525519; DOI=10.1128/jb.167.2.695-702.1986; RA Follettie M.T., Sinskey A.J.; RT "Molecular cloning and nucleotide sequence of the Corynebacterium RT glutamicum pheA gene."; RL J. Bacteriol. 167:695-702(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / RC LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / RC LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). CC -!- CATALYTIC ACTIVITY: CC Reaction=prephenate + H(+) = 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 -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; CC phenylpyruvate from prephenate: step 1/1. 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; M13774; AAA23304.1; -; Genomic_DNA. DR EMBL; BA000036; BAC00293.1; -; Genomic_DNA. DR EMBL; BX927156; CAF20922.1; -; Genomic_DNA. DR PIR; A26044; A26044. DR RefSeq; WP_003862609.1; NC_003450.3. DR AlphaFoldDB; P10341; -. DR SMR; P10341; -. DR STRING; 196627.cg3207; -. DR PaxDb; 196627-cg3207; -. DR GeneID; 1020842; -. DR KEGG; cgb:cg3207; -. DR KEGG; cgl:Cgl2899; -. DR PATRIC; fig|196627.13.peg.2829; -. DR eggNOG; COG0077; Bacteria. DR HOGENOM; CLU_035008_0_0_11; -. DR OMA; AACMHGI; -. DR OrthoDB; 9802281at2; -. DR BioCyc; CORYNE:G18NG-12517-MONOMER; -. DR SABIO-RK; P10341; -. DR UniPathway; UPA00121; UER00345. DR Proteomes; UP000000582; Chromosome. DR AbasyAtlas; P10341; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd04905; ACT_CM-PDT; 1. DR CDD; cd13632; PBP2_Aa-PDT_like; 1. DR FunFam; 3.30.70.260:FF:000012; Prephenate dehydratase; 1. DR Gene3D; 3.30.70.260; -; 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; IPR001086; Preph_deHydtase. DR InterPro; IPR018528; Preph_deHydtase_CS. DR NCBIfam; NF008865; pheA; 1. DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1. DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00800; PDT; 1. DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1. DR SUPFAM; SSF55021; ACT-like; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR PROSITE; PS51671; ACT; 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; Aromatic amino acid biosynthesis; Lyase; KW Phenylalanine biosynthesis; Reference proteome. FT CHAIN 1..315 FT /note="Prephenate dehydratase" FT /id="PRO_0000119177" FT DOMAIN 7..190 FT /note="Prephenate dehydratase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517" FT DOMAIN 204..283 FT /note="ACT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007" FT SITE 183 FT /note="Essential for activity" FT /evidence="ECO:0000250" FT CONFLICT 99 FT /note="M -> S (in Ref. 1; AAA23304)" FT /evidence="ECO:0000305" FT CONFLICT 224 FT /note="A -> G (in Ref. 1; AAA23304)" FT /evidence="ECO:0000305" SQ SEQUENCE 315 AA; 33740 MW; 8D7F0B1F06851112 CRC64; MSDAPTVVAY LGPAGTFTEE ALYKFADAGV FGDGEIEQLP AKSPQEAVDA VRHGTAQFAV VAIENFVDGP VTPTFDALDQ GSNVQIIAEE ELDIAFSIMV RPGTSLADVK TLATHPVGYQ QVKNWMATTI PDAMYLSASS NGAGAQMVAE GTADAAAAPS RAAELFGLER LVDDVADVRG ARTRFVAVQA QAAVSEPTGH DRTSVIFSLP NVPGSLVRAL NEFAIRGVDL TRIESRPTRK VFGTYRFHLD ISGHIRDIPV AEALRALHLQ AEELVFVGSW PSNRAEDSTP QTDQLAKLHK ADEWVRAASE GRKLN //