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Database: UniProt
Entry: A0A1Q5M858_9ACTN
LinkDB: A0A1Q5M858_9ACTN
Original site: A0A1Q5M858_9ACTN 
ID   A0A1Q5M858_9ACTN        Unreviewed;       310 AA.
AC   A0A1Q5M858;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN   ORFNames=AMK33_15150 {ECO:0000313|EMBL:OKK10265.1};
OS   Streptomyces sp. CB02400.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703944 {ECO:0000313|EMBL:OKK10265.1, ECO:0000313|Proteomes:UP000185993};
RN   [1] {ECO:0000313|EMBL:OKK10265.1, ECO:0000313|Proteomes:UP000185993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02400 {ECO:0000313|EMBL:OKK10265.1,
RC   ECO:0000313|Proteomes:UP000185993};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(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:OKK10265.1}.
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DR   EMBL; LIWB01000005; OKK10265.1; -; Genomic_DNA.
DR   RefSeq; WP_073933379.1; NZ_LIWB01000005.1.
DR   AlphaFoldDB; A0A1Q5M858; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000185993; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185993}.
FT   DOMAIN          4..182
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          197..274
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            175
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   310 AA;  33555 MW;  858DFAA0EEA38D44 CRC64;
     MPASYAYLGP EGTFTEVALR TLPEAATREL IPYVSVQSAL DAVRTGEAEA AFVPIENSVE
     GGITTTLDEL VAGTPLMIYR EVLLSITFAL LVRPGTKLSD IKTVTAHPAA QPQVRNWLKT
     HLPDAVWESA ASNADGARLV QEGRYDAAFA GEFAAARYGL EALETEIHDA ENAQTRFVLV
     GRPARPAAPT GADKTSVVLW QRDDHPGGLR DLLGEFATRG INLMLLQSRP TGAGIGNYCF
     CIDAEGHISD RRMAEALMGL KRICLQVRFL GSYPRADVRP GEVRPPFPGT SDEEFVGAAD
     WVARCQDGRF
//
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