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Database: UniProt
Entry: A0A024FES7_9FLAO
LinkDB: A0A024FES7_9FLAO
Original site: A0A024FES7_9FLAO 
ID   A0A024FES7_9FLAO        Unreviewed;       275 AA.
AC   A0A024FES7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=prephenate dehydratase {ECO:0000256|ARBA:ARBA00013147};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN   ORFNames=WPG_0725 {ECO:0000313|EMBL:BAO74955.1};
OS   Winogradskyella sp. PG-2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO74955.1, ECO:0000313|Proteomes:UP000031636};
RN   [1] {ECO:0000313|EMBL:BAO74955.1, ECO:0000313|Proteomes:UP000031636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-2 {ECO:0000313|EMBL:BAO74955.1,
RC   ECO:0000313|Proteomes:UP000031636};
RX   PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA   Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT   "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT   Proteorhodopsin-Containing Marine Flavobacterium.";
RL   Genome Announc. 2:e00490-14(2014).
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}.
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DR   EMBL; AP014583; BAO74955.1; -; Genomic_DNA.
DR   RefSeq; WP_045469441.1; NZ_AP014583.1.
DR   AlphaFoldDB; A0A024FES7; -.
DR   STRING; 754409.WPG_0725; -.
DR   KEGG; win:WPG_0725; -.
DR   HOGENOM; CLU_035008_1_0_10; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000031636; Chromosome.
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; cd13631; PBP2_Ct-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; IPR001086; Preph_deHydtase.
DR   PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR   PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF00800; PDT; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS51671; ACT; 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:UP000031636}.
FT   DOMAIN          4..181
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          195..275
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   275 AA;  31150 MW;  76A8FC66D4A34C6A CRC64;
     MTKPIAIQGI KGSFHHEVAQ VYFSDKAEIV ECMSFDGTVN HLLNGDTDHI VMALENSIAG
     SIIPNYALID THNLSIVGEH YLDIQHNLLA LNGQSITEIK EVHSHPMALL QCKVFFKKYS
     HIKLVEAQDT ADVAKQISDQ NLKGIAAIAS KNAAKIYELD VLEESIQTIK HNETRFVIVK
     REIQITERKE LNKASLKFEL DHKRGSLATI LNVMSDCKLN LTKIQSLPKI ETPWKYAFFV
     DVTFEDYKDY EKASSIMQLM AENFKVLGEY KNARL
//
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