BACA_BACSU
ID BACA_BACSU Reviewed; 204 AA.
AC P39638;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Prephenate decarboxylase {ECO:0000303|PubMed:20052993};
DE EC=4.1.1.100 {ECO:0000269|PubMed:20052993, ECO:0000269|PubMed:22483065};
DE AltName: Full=Bacilysin biosynthesis protein BacA {ECO:0000303|PubMed:15609023};
DE AltName: Full=Non-aromatizing prephenate decarboxylase {ECO:0000303|PubMed:20052993};
GN Name=bacA {ECO:0000303|PubMed:15609023};
GN Synonyms=ywfB {ECO:0000303|PubMed:15609023}; OrderedLocusNames=BSU37740;
GN ORFNames=ipa-80d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION, AND PATHWAY.
RC STRAIN=168 / 61884;
RX PubMed=12372825; DOI=10.1074/jbc.m208722200;
RA Inaoka T., Takahashi K., Ohnishi-Kameyama M., Yoshida M., Ochi K.;
RT "Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-
RT operatively regulate the production of an antibiotic bacilysin in Bacillus
RT subtilis.";
RL J. Biol. Chem. 278:2169-2176(2003).
RN [4]
RP FUNCTION IN BACILYSIN PRODUCTION, AND GENE NAME.
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND REACTION MECHANISM.
RC STRAIN=168;
RX PubMed=20052993; DOI=10.1021/bi9021186;
RA Mahlstedt S.A., Walsh C.T.;
RT "Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to
RT tetrahydrotyrosine in Bacillus subtilis.";
RL Biochemistry 49:912-923(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=168;
RX PubMed=22483065; DOI=10.1021/bi300254u;
RA Parker J.B., Walsh C.T.;
RT "Olefin isomerization regiochemistries during tandem action of BacA and
RT BacB on prephenate in bacilysin biosynthesis.";
RL Biochemistry 51:3241-3251(2012).
RN [7]
RP FUNCTION, AND PATHWAY.
RX PubMed=22765234; DOI=10.1021/bi3006362;
RA Parker J.B., Walsh C.T.;
RT "Stereochemical outcome at four stereogenic centers during conversion of
RT prephenate to tetrahydrotyrosine by BacABGF in the bacilysin pathway.";
RL Biochemistry 51:5622-5632(2012).
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
CC (PubMed:15609023, PubMed:20052993). BacA is an unusual prephenate
CC decarboxylase that avoids the typical aromatization of the
CC cyclohexadienol ring of prephenate (PubMed:20052993)(PubMed:22483065).
CC BacA catalyzes the protonation of prephenate (1-carboxy-4-hydroxy-
CC alpha-oxo-2,5-cyclohexadiene-1-propanoic acid) at C6 position, followed
CC by a decarboxylation to produce the endocyclic-delta(4),delta(8)-7R-
CC dihydro-hydroxyphenylpyruvate (en-H2HPP) (PubMed:20052993,
CC PubMed:22483065, PubMed:22765234). En-H2HPP is able to undergo a slow
CC nonenzymatic isomerization to produce the exocyclic-delta(3),delta(5)-
CC dihydro-hydroxyphenylpyruvate (ex-H2HPP)
CC (PubMed:20052993)(PubMed:22483065). BacA isomerizes only the pro-R
CC double bond in prephenate (PubMed:22483065).
CC {ECO:0000269|PubMed:15609023, ECO:0000269|PubMed:20052993,
CC ECO:0000269|PubMed:22483065, ECO:0000269|PubMed:22765234}.
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:0000269|PubMed:20052993,
CC ECO:0000269|PubMed:22483065};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for prephenate {ECO:0000269|PubMed:20052993};
CC Note=kcat is 190 min(-1) for decarboxylase activity with prephenate
CC as substrate. {ECO:0000269|PubMed:20052993};
CC -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC {ECO:0000269|PubMed:22765234, ECO:0000305|PubMed:12372825}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp)
CC is essential for the transcription of the bacABCDEF operon and BacG,
CC and GTP regulates the transcription of both this operon and ywfH via
CC the CodY-mediated regulation system. {ECO:0000269|PubMed:12372825}.
CC -!- SIMILARITY: Belongs to the prephenate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X73124; CAA51636.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15801.1; -; Genomic_DNA.
DR PIR; S39735; S39735.
DR RefSeq; NP_391654.1; NC_000964.3.
DR RefSeq; WP_009968341.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39638; -.
DR SMR; P39638; -.
DR STRING; 224308.BSU37740; -.
DR PaxDb; P39638; -.
DR PRIDE; P39638; -.
DR EnsemblBacteria; CAB15801; CAB15801; BSU_37740.
DR GeneID; 937216; -.
DR KEGG; bsu:BSU37740; -.
DR PATRIC; fig|224308.179.peg.4086; -.
DR eggNOG; COG0077; Bacteria.
DR OMA; INIDTHH; -.
DR BioCyc; BSUB:BSU37740-MON; -.
DR BioCyc; MetaCyc:MON-19126; -.
DR BRENDA; 4.1.1.100; 658.
DR UniPathway; UPA00100; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..204
FT /note="Prephenate decarboxylase"
FT /id="PRO_0000064797"
SQ SEQUENCE 204 AA; 23326 MW; BFA6B79CFFA6A96F CRC64;
MIILDNSIQT KKRTDSLSKL ITVNTLGPEG TSSEYAAKHF ISNFTLLQGL NSKLSLHDTF
ESCIERTLQS PLEYTIVPHA YDGIKHFYMR PDLQLLQIFR CDTPMYGLAV RPDFEFRDDM
LDTSVIVSHP SPINLIKYFT RKDVRFKLVN STSQAARKVK EGLYDIALTN ELARQKYGLT
FVKTFKSIPM SWSLFGKGDV DDEN
