PHEA_MYCSK
ID PHEA_MYCSK Reviewed; 315 AA.
AC A1UNA3;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=Mkms_5122;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; CP000518; ABL94311.1; -; Genomic_DNA.
DR RefSeq; WP_011562409.1; NC_008705.1.
DR AlphaFoldDB; A1UNA3; -.
DR SMR; A1UNA3; -.
DR STRING; 189918.Mkms_5122; -.
DR EnsemblBacteria; ABL94311; ABL94311; Mkms_5122.
DR KEGG; mkm:Mkms_5122; -.
DR HOGENOM; CLU_035008_0_0_11; -.
DR OMA; PLMIYRE; -.
DR OrthoDB; 1280729at2; -.
DR UniPathway; UPA00121; UER00345.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Phenylalanine biosynthesis.
FT CHAIN 1..315
FT /note="Prephenate dehydratase"
FT /id="PRO_0000382041"
FT DOMAIN 3..190
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 204..281
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT SITE 183
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 32736 MW; 95A1B1B47B7B2669 CRC64;
MPRIAYLGPQ GTFTESALLQ MISGAMVPGG DADDTAVTPV PTDSTPAGLE AVRSGAADYA
CVPIENSIEG SVLPTLDSLA VGAPLQIFAE LTLAVSFSIV VRPDHDGDVG TVAAFPVAAA
QVRRWLAEHL PAAQLVPAHS NAAAAADVAG GRADAGISTA LAAERYGLRS LAAGVVDEPN
ARTRFVLVGR PAPPPARTGA DRTSVALRLP NTPGALVAAM TELSIRDIDL TRIESRPTRT
ELGTYVFFLD CVGHLEDDAV AEALKALHRR CEDVRYLGSW PTGTAAGAPP PSSDEATRWL
TRLREGLPTP PEGGR
