ID A0A1G7N0R5_9ACTN Unreviewed; 314 AA.
AC A0A1G7N0R5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872, 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 ORFNames=SAMN05660662_3030 {ECO:0000313|EMBL:SDF67552.1};
OS Blastococcus aurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1550231 {ECO:0000313|EMBL:SDF67552.1, ECO:0000313|Proteomes:UP000199406};
RN [1] {ECO:0000313|EMBL:SDF67552.1, ECO:0000313|Proteomes:UP000199406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44268 {ECO:0000313|EMBL:SDF67552.1,
RC ECO:0000313|Proteomes:UP000199406};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNBT01000005; SDF67552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7N0R5; -.
DR STRING; 1550231.SAMN05660662_3030; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000199406; Unassembled WGS sequence.
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; cd13632; PBP2_Aa-PDT_like; 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 9..187
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 201..278
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 180
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 314 AA; 32724 MW; 92937DE9BDBE51DE CRC64;
MQPSTSPTRF AYLGPEGTFA EAALSSVIDT GEGTRNPRSS VPATLAAVRS GDADAGLVPL
ENSVEGSVPA TMDGLADGDP LVITREVFLP VAFTLAVRPG TTLADVRSVA SHPHALAQTG
RWLEANLPGI TPLPASSTAG AAAAVAAGEY DAAVCAAIAA QRYGLDALAE GIADHAGAVT
RFVLVARPGP LPAPTGNDKT SLVAVVTDRT GALLDVLREF AVRGISLTRI ESRPLRDRLW
VYSFFLDCEG HIADRRVGEA LAALHRVCED VRFLGSYPRS DGRENRAVED ESADDAFAEA
EGWLARVRAG DLGG
//
