PHEA_MYCVP
ID PHEA_MYCVP Reviewed; 312 AA.
AC A1TGX7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=Mvan_5662;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
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}.
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; CP000511; ABM16427.1; -; Genomic_DNA.
DR RefSeq; WP_011782779.1; NC_008726.1.
DR AlphaFoldDB; A1TGX7; -.
DR SMR; A1TGX7; -.
DR STRING; 350058.Mvan_5662; -.
DR PRIDE; A1TGX7; -.
DR EnsemblBacteria; ABM16427; ABM16427; Mvan_5662.
DR KEGG; mva:Mvan_5662; -.
DR eggNOG; COG0077; Bacteria.
DR HOGENOM; CLU_035008_0_0_11; -.
DR OMA; PLMIYRE; -.
DR OrthoDB; 1280729at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000009159; 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: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; 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; Reference proteome.
FT CHAIN 1..312
FT /note="Prephenate dehydratase"
FT /id="PRO_0000382045"
FT DOMAIN 3..194
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 208..285
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 291..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 187
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 312 AA; 32278 MW; BEEAD55A2A735322 CRC64;
MPGIAYLGPE GTFTEAALRA LQAHGLIPST APDAAGADEV TPIAADSTSA ALAAVRSGDA
DFACVPIENS IDGSVIPTLD SLADGAALQI YAELTLDVSF TIAVRPGTAA ADVRTVAAYP
VAAAQVRRWL AAHLPEAEVV PANSNAAAAQ DVAAGRADAG VSTALATQRY GLEALAADVV
DEPNARTRFV LVGRPGPPPK CTGADRTSVV LQLDNVPGAL VSAMTELAVR DIDLTRIESR
PTRTGLGTYK FFLDFVGHIE DPPVAEALRA LHRRCADVRY LGSWPTGDVV GAAPPPMDES
ASWLEGLREG RP
