ID A0A2U1T248_9MICO Unreviewed; 315 AA.
AC A0A2U1T248;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN ORFNames=DF220_09015 {ECO:0000313|EMBL:PWB97954.1};
OS Salinibacterium hongtaonis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Salinibacterium.
OX NCBI_TaxID=2079791 {ECO:0000313|EMBL:PWB97954.1, ECO:0000313|Proteomes:UP000244978};
RN [1] {ECO:0000313|Proteomes:UP000244978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1194 {ECO:0000313|Proteomes:UP000244978};
RA Liu S., Wang Z., Li J.;
RL Submitted (APR-2018) 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 -!- 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:PWB97954.1}.
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DR EMBL; QEEX01000001; PWB97954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1T248; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000244978; 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:UP000244978}.
FT DOMAIN 9..188
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 203..281
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 181
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 315 AA; 33517 MW; F778394FB404FB90 CRC64;
MPDSPREQTY SYLGPAGTFT EAALAQVPEA QGKTWRAVNN VGEALGDVLE GRSVAAMIAI
ENSVDGGVSA TQDALATMTG LRIVGEYLVS VNFVLVARPG TTLADVRVIN AHPVAYAQCS
RWLGANLASH GHIPATSNVA AAASLFENAQ ADAAIAPPGI TAHYDLDVLA EGIGDNPNAV
TRFVLVSRTA PVPERTGSDK TSIIAELPDN KAGRLLEMLE QFATRGVNMS LIESRPIGDE
LGRYRFVIDL EGHILDERVA DALLGLKRFS PNVIFLGSYP RADRARPTVT PRYEDAAFTD
ARDWLRGLIA GEPAA
//