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Database: UniProt
Entry: B1MEG8
LinkDB: B1MEG8
Original site: B1MEG8 
ID   PHEA_MYCA9              Reviewed;         308 AA.
AC   B1MEG8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Prephenate dehydratase;
DE            Short=PDT;
DE            EC=4.2.1.51;
GN   Name=pheA; OrderedLocusNames=MAB_0132;
OS   Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS   13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=561007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC   1543;
RX   PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA   Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA   Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA   Gaillard J.L.;
RT   "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT   Mycobacterium abscessus.";
RL   PLoS ONE 4:E5660-E5660(2009).
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; CU458896; CAM60232.1; -; Genomic_DNA.
DR   RefSeq; WP_005062863.1; NZ_MLCG01000005.1.
DR   AlphaFoldDB; B1MEG8; -.
DR   SMR; B1MEG8; -.
DR   EnsemblBacteria; CAM60232; CAM60232; MAB_0132.
DR   GeneID; 66970516; -.
DR   KEGG; mab:MAB_0132; -.
DR   OMA; PLMIYRE; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000007137; 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.
FT   CHAIN           1..308
FT                   /note="Prephenate dehydratase"
FT                   /id="PRO_0000382030"
FT   DOMAIN          3..187
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT   DOMAIN          201..278
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   SITE            180
FT                   /note="Essential for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  32178 MW;  7D02AB44EB0D724F CRC64;
     MQRITYLGPE GTFSEAAMIT LRTTGRIPGS SEVEPVSVAS AREALVQVQA GDADYACVPI
     ESSLEGPVVP TLDTLAVGAP LQIFAETVLP VSFTIAVRPG TAAGDVKTVA GFPIAAAQVR
     EWLATNLPDA ELVAANSNAA AAEDVKAERA DAGVCTEWAA QRLGLHALAS GVVDEAHAHT
     RFVLVGRPGP PPAATGADRT SVVLGLGNVP GALAAAMNEF AIRDIDLTRI ESRPTRTGLG
     TYRFFLDCVG HIDDIAVGEA LKGLHRRCED VRYLGSWPRG TTAPTGANPP VLDEASGWLA
     ETREGRLR
//
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