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Database: UniProt
Entry: P10341
LinkDB: P10341
Original site: P10341 
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   03-AUG-2022, entry version 130.
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 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   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 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
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 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
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=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   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
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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; NP_602088.1; NC_003450.3.
DR   RefSeq; WP_003862609.1; NC_006958.1.
DR   AlphaFoldDB; P10341; -.
DR   SMR; P10341; -.
DR   STRING; 196627.cg3207; -.
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; PLMIYRE; -.
DR   SABIO-RK; P10341; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
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   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SUPFAM; SSF55021; SSF55021; 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
//
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