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Database: UniProt
Entry: A0A2I1J8R6_9MICC
LinkDB: A0A2I1J8R6_9MICC
Original site: A0A2I1J8R6_9MICC 
ID   A0A2I1J8R6_9MICC        Unreviewed;       316 AA.
AC   A0A2I1J8R6;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=CJ193_02975 {ECO:0000313|EMBL:PMC78477.1}, CYJ35_08380
GN   {ECO:0000313|EMBL:PKY79781.1};
OS   Pseudoglutamicibacter albus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudoglutamicibacter.
OX   NCBI_TaxID=98671 {ECO:0000313|EMBL:PKY79781.1, ECO:0000313|Proteomes:UP000234591};
RN   [1] {ECO:0000313|EMBL:PMC78477.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMB0715 {ECO:0000313|EMBL:PMC78477.1};
RA   Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT   "Bacterial strain isolated from the female urinary microbiota.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PKY79781.1, ECO:0000313|Proteomes:UP000234591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMB0722 {ECO:0000313|EMBL:PKY79781.1,
RC   ECO:0000313|Proteomes:UP000234591};
RA   Thomas-White K., Wolfe A.J.;
RT   "Phylogenetic diversity of female urinary microbiome.";
RL   Submitted (DEC-2017) 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}.
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:PKY79781.1}.
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DR   EMBL; PKGR01000010; PKY79781.1; -; Genomic_DNA.
DR   EMBL; PNHO01000005; PMC78477.1; -; Genomic_DNA.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000234591; 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; 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          5..189
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          204..281
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            182
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   316 AA;  33695 MW;  A2EB633E4469A179 CRC64;
     MATVKYTYLG PAGTFCEQAL LTLPGPAAEP EHNRIPATNV DVALQLVRDG EVDAAVVPIE
     NSVEGGVSAT LDSIAAGDSL HIVAEAVIPV TFQLAALPGI ESLEEIRTIS THGHAWAQCR
     QWAQNTIPNV DFLPASSTAA GALGLLEENP AYQAAICSPL VAERHNLNVL AEGIEDNQGA
     VTRFVMVQKP GRIPEATGSD KSTIVVELTH DRPGGLREIL DHFATRGVNL TRIESRPTGT
     GLGQYFFSID LEGHISEPRV EEVLHGLHRI STYIRYLGSY PSATPVVVNV PPHATPEAYQ
     AADAWLNEIL EGGNPA
//
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