ID Q118Y8_TRIEI Unreviewed; 296 AA.
AC Q118Y8;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
DE Short=PDT {ECO:0000256|RuleBase:RU361254};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
GN Name=pheA {ECO:0000256|RuleBase:RU361254};
GN OrderedLocusNames=Tery_0480 {ECO:0000313|EMBL:ABG49936.1};
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG49936.1};
RN [1] {ECO:0000313|EMBL:ABG49936.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG49936.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000913,
CC ECO:0000256|RuleBase:RU361254};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741, ECO:0000256|RuleBase:RU361254}.
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DR EMBL; CP000393; ABG49936.1; -; Genomic_DNA.
DR AlphaFoldDB; Q118Y8; -.
DR STRING; 203124.Tery_0480; -.
DR KEGG; ter:Tery_0480; -.
DR eggNOG; COG0077; Bacteria.
DR HOGENOM; CLU_035008_0_2_3; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13630; PBP2_PDT_1; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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 PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF00800; PDT; 1.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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 {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU361254};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU361254};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361254};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222,
KW ECO:0000256|RuleBase:RU361254}.
FT DOMAIN 4..186
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 214..291
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 179
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 296 AA; 32619 MW; F500A018BAD2100C CRC64;
MTISIAHLGP AGTYTETAAV AFSEKLGQHG QKSILCPYPS IAQTLSAVSQ EQVNLAVVPV
ENSIEGSVTV TLDTLWKLDI LEIQTALVLP ISHGLISLAT SFEEIKIVYS HPQALAQCQG
WLEKFLPQVK QVPANSTTEA LEHLEKERSA GAIASHRAAK IYKLPVLAYP INDYSDNCTR
FLVLKKGCTE MENSAFKLII NTRDKPENLV FTSLGFTVPA NEPGALVKPL QVFAKREINM
SRIESRPTKL SLGDYLFFID IEANINHNSV KVAIEELKTY TQTLKIFGSY ILMSIN
//