PHEA_BACSU
ID PHEA_BACSU Reviewed; 285 AA.
AC P21203;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=BSU27900;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2537815; DOI=10.1128/jb.171.3.1362-1371.1989;
RA Trach K., Hoch J.A.;
RT "The Bacillus subtilis spo0B stage 0 sporulation operon encodes an
RT essential GTP-binding protein.";
RL J. Bacteriol. 171:1362-1371(1989).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-285.
RC STRAIN=168;
RX PubMed=8444804; DOI=10.1128/jb.175.5.1423-1432.1993;
RA Sun D., Setlow P.L.;
RT "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB
RT gene and a nifS-like gene, both of which are essential for NAD
RT biosynthesis.";
RL J. Bacteriol. 175:1423-1432(1993).
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.
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DR EMBL; M24537; AAA22507.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14750.1; -; Genomic_DNA.
DR EMBL; M98822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C32804; C32804.
DR RefSeq; NP_390668.1; NC_000964.3.
DR RefSeq; WP_004398512.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P21203; -.
DR SMR; P21203; -.
DR STRING; 224308.BSU27900; -.
DR PaxDb; P21203; -.
DR PRIDE; P21203; -.
DR EnsemblBacteria; CAB14750; CAB14750; BSU_27900.
DR GeneID; 937513; -.
DR KEGG; bsu:BSU27900; -.
DR PATRIC; fig|224308.179.peg.3031; -.
DR eggNOG; COG0077; Bacteria.
DR InParanoid; P21203; -.
DR OMA; HTRFVIL; -.
DR PhylomeDB; P21203; -.
DR BioCyc; BSUB:BSU27900-MON; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IBA:GO_Central.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IBA:GO_Central.
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; PF00800; PDT; 1.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Phenylalanine biosynthesis; Reference proteome.
FT CHAIN 1..285
FT /note="Prephenate dehydratase"
FT /id="PRO_0000119176"
FT DOMAIN 2..183
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 204..281
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT SITE 176
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 285 AA; 31901 MW; A480D3F931906EEF CRC64;
MKVGYLGPAA TFTHLAVSSC FQNGAEHVAY RTIPECIDAA VAGEVDFAFV PLENALEGSV
NLTIDYLIHE QPLPIVGEMT LPIHQHLLVH PSRENAWKEL DKIYSHSHAI AQCHKFLHRH
FPSVPYEYAN STGAAAKFVS DHPELNIGVI ANDMAASTYE LKIVKRDIQD YRDNHTRFVI
LSPDENISFE VNSKLSSRPK TTLMVMLPQD DQSGALHRVL SAFSWRNLNL SKIESRPTKT
GLGHYFFIID IEKAFDDVLI PGAMQELEAL GCKVRLLGAY QSYQL
