PHEA_MYCBO
ID PHEA_MYCBO Reviewed; 321 AA.
AC Q7TVJ6; A0A1R3Y5E0; X2BPX4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=BQ2027_MB3868C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC STRAIN=BCG / Pasteur;
RX PubMed=16006064; DOI=10.1016/j.femsle.2005.06.004;
RA Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y.;
RT "Thiol specific oxidative stress response in Mycobacteria.";
RL FEMS Microbiol. Lett. 249:87-94(2005).
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 -!- INDUCTION: Induced in response to the thiol oxidant diamide.
CC {ECO:0000269|PubMed:16006064}.
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; LT708304; SIU02497.1; -; Genomic_DNA.
DR RefSeq; NP_857505.1; NC_002945.3.
DR RefSeq; WP_003420906.1; NC_002945.4.
DR AlphaFoldDB; Q7TVJ6; -.
DR SMR; Q7TVJ6; -.
DR EnsemblBacteria; SIU02497; SIU02497; BQ2027_MB3868C.
DR PATRIC; fig|233413.5.peg.4230; -.
DR OMA; PLMIYRE; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000001419; 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; 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; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Phenylalanine biosynthesis.
FT CHAIN 1..321
FT /note="Prephenate dehydratase"
FT /id="PRO_0000382032"
FT DOMAIN 3..189
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 203..280
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT SITE 182
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 33633 MW; A50F13226F788EE5 CRC64;
MVRIAYLGPE GTFTEAALVR MVAAGLVPET GPDALQRMPV ESAPAALAAV RDGGADYACV
PIENSIDGSV LPTLDSLAIG VRLQVFAETT LDVTFSIVVK PGRNAADVRT LAAFPVAAAQ
VRQWLAAHLP AADLRPAYSN ADAARQVADG LVDAAVTSPL AAARWGLAAL ADGVVDESNA
RTRFVLVGRP GPPPARTGAD RTSAVLRIDN QPGALVAALA EFGIRGIDLT RIESRPTRTE
LGTYLFFVDC VGHIDDEAVA EALKAVHRRC ADVRYLGSWP TGPAAGAQPP LVDEASRWLA
RLRAGKPEQT LVRPDDQGAQ A