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Database: UniProt
Entry: B2HMM5
LinkDB: B2HMM5
Original site: B2HMM5 
ID   PHEA_MYCMM              Reviewed;         315 AA.
AC   B2HMM5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=MMAR_5390;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC43794.1; -; Genomic_DNA.
DR   RefSeq; WP_012396890.1; NC_010612.1.
DR   AlphaFoldDB; B2HMM5; -.
DR   SMR; B2HMM5; -.
DR   STRING; 216594.MMAR_5390; -.
DR   EnsemblBacteria; ACC43794; ACC43794; MMAR_5390.
DR   KEGG; mmi:MMAR_5390; -.
DR   eggNOG; COG0077; Bacteria.
DR   HOGENOM; CLU_035008_0_0_11; -.
DR   OMA; PLMIYRE; -.
DR   OrthoDB; 1280729at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000001190; 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   3: Inferred from homology;
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_0000382037"
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   315 AA;  32783 MW;  3185DE295D89A989 CRC64;
     MARIAYLGPE GTFTQAALLE IAAAGLVPGH DDGGAQPLPV ESTPAALDAV RTGAAEFACV
     PIENSIDGSL APTLDSLAIG SPLQVFAETT LDVAFSIVVR PGVGAADVRT LAAFPVAAAQ
     VRQWLTAHLP SVELHPAYSN ADAARQVAEG QVDAAVTSPL AAAHWALQSL ADGVVDESNA
     RTRFLLIGVP GPPPPRTGTD RTSVVLRIAN VPGALLDALT EFGMRGIDLT RIESRPTRTG
     LGTYMFFVDC VGHIADDAVA EALKALHRRC ADVRYLGSWP TGQTYAGQPP PADEAAIWLQ
     QLREGKPEAS PGPPL
//
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