PHEA_MYCMM
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
