ID A0A1E7L7J4_9ACTN Unreviewed; 309 AA.
AC A0A1E7L7J4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN ORFNames=AN218_09440 {ECO:0000313|EMBL:OEV12187.1};
OS Streptomyces nanshensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=518642 {ECO:0000313|EMBL:OEV12187.1, ECO:0000313|Proteomes:UP000176005};
RN [1] {ECO:0000313|EMBL:OEV12187.1, ECO:0000313|Proteomes:UP000176005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10429 {ECO:0000313|EMBL:OEV12187.1,
RC ECO:0000313|Proteomes:UP000176005};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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 -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEV12187.1}.
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DR EMBL; LJGW01000156; OEV12187.1; -; Genomic_DNA.
DR RefSeq; WP_070016316.1; NZ_LJGW01000156.1.
DR AlphaFoldDB; A0A1E7L7J4; -.
DR PATRIC; fig|518642.10.peg.1884; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000176005; Unassembled WGS sequence.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
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; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT DOMAIN 6..184
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 199..276
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 177
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 309 AA; 33205 MW; 6C3938C89E8159CF CRC64;
MPPASRFTYL GPEGTFTEAA LRTLPETATR ELTPMVSVPA ALDAVRNGEA AAAFVPIENS
VEGGVTATLD ELAGGRPLMI YREVLLPIAF ALLARPGTTL EGIKTVTGHP VAQPQVRRWV
ADNLPYALWE SAASNADGAR LVQEGRYDAA FAGEFAAATY GLEPLVTDIH DADNAATRFV
LVGRPARPAA PTGSDKTSVV FWLRDDHPGA LLEVLQEFAS RGVNMMRIES RPTGEGIGRY
CFSVDCEGHL QDRRVGDVLM GLKRACEQVR YLGSYPRADG GRSGERPGTT DAEFMEAADW
LARCLDGRG
//
