ID   BACA_BACIU              Reviewed;         204 AA.
AC   Q8KWT6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Prephenate decarboxylase {ECO:0000250|UniProtKB:P39638};
DE            EC=4.1.1.100 {ECO:0000250|UniProtKB:P39638};
DE   AltName: Full=Bacilysin biosynthesis protein BacA {ECO:0000250|UniProtKB:P39638};
DE   AltName: Full=Non-aromatizing prephenate decarboxylase {ECO:0000250|UniProtKB:P39638};
GN   Name=bacA {ECO:0000250|UniProtKB:P39638};
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A1/3;
RX   PubMed=15609023; DOI=10.1007/s00203-004-0743-8;
RA   Steinborn G., Hajirezaei M.-R., Hofemeister J.;
RT   "bac genes for recombinant bacilysin and anticapsin production in Bacillus
RT   host strains.";
RL   Arch. Microbiol. 183:71-79(2005).
CC   -!- FUNCTION: Part of the bacABCDEF operon responsible for the biosynthesis
CC       of the nonribosomally synthesized dipeptide antibiotic bacilysin,
CC       composed of L-alanine and L-anticapsin. Bacilysin is an irreversible
CC       inactivator of the glutaminase domain of glucosamine synthetase. BacA
CC       is an unusual prephenate decarboxylase that avoids the typical
CC       aromatization of the cyclohexadienol ring of prephenate. BacA catalyzes
CC       the protonation of prephenate (1-carboxy-4-hydroxy-alpha-oxo-2,5-
CC       cyclohexadiene-1-propanoic acid) at C6 position, followed by a
CC       decarboxylation to produce the endocyclic-delta(4),delta(8)-7R-dihydro-
CC       hydroxyphenylpyruvate (en-H2HPP). En-H2HPP is able to undergo a slow
CC       nonenzymatic isomerization to produce the exocyclic-delta(3),delta(5)-
CC       dihydro-hydroxyphenylpyruvate (ex-H2HPP). BacA isomerizes only the pro-
CC       R double bond in prephenate. {ECO:0000250|UniProtKB:P39638}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-
CC         2-oxopropanoate + CO2; Xref=Rhea:RHEA:33499, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:29934, ChEBI:CHEBI:84354;
CC         EC=4.1.1.100; Evidence={ECO:0000250|UniProtKB:P39638};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC       {ECO:0000250|UniProtKB:P39638}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the prephenate decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF396778; AAM90568.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KWT6; -.
DR   SMR; Q8KWT6; -.
DR   UniPathway; UPA00100; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; ISS:UniProtKB.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Cytoplasm; Lyase.
FT   CHAIN           1..204
FT                   /note="Prephenate decarboxylase"
FT                   /id="PRO_0000064795"
SQ   SEQUENCE   204 AA;  23022 MW;  74591E9A59A474DD CRC64;
     MIILDNSIQT KSKAYSISKL ITINTLGPEG TSSEYAAKNF ITNFTLLQGV NSKLSLHDTF
     ESCIEKTLQS PLEYTIVPHA YDGIKHFYMR PDLQLLQIFR CDTPMYGLAV RPGFEYTDDM
     LDKAVIVSHP SPINLIKYFT RKDVTFDLVN STSAAAKRVK DGLSDIALTN ELARQKYGLH
     FVKTFKSIPM SWSLFGKGEI HDEN