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Database: UniProt
Entry: A0A1H8AWM6_9MICO
LinkDB: A0A1H8AWM6_9MICO
Original site: A0A1H8AWM6_9MICO 
ID   A0A1H8AWM6_9MICO        Unreviewed;       318 AA.
AC   A0A1H8AWM6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN   Name=pheA {ECO:0000313|EMBL:TFB88658.1};
GN   ORFNames=E3O10_12890 {ECO:0000313|EMBL:TFB88658.1};
OS   Cryobacterium luteum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1424661 {ECO:0000313|EMBL:TFB88658.1, ECO:0000313|Proteomes:UP000297654};
RN   [1] {ECO:0000313|EMBL:TFB88658.1, ECO:0000313|Proteomes:UP000297654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh15 {ECO:0000313|EMBL:TFB88658.1,
RC   ECO:0000313|Proteomes:UP000297654};
RA   Liu Q., Xin Y.-H.;
RT   "Genomics of glacier-inhabiting Cryobacterium strains.";
RL   Submitted (MAR-2019) 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:TFB88658.1}.
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DR   EMBL; SOFF01000031; TFB88658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8AWM6; -.
DR   STRING; 1424661.SAMN05216281_101361; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000297654; 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   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; 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, ECO:0000313|EMBL:TFB88658.1};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
SQ   SEQUENCE   318 AA;  33997 MW;  8AFE8B595EEBBE3F CRC64;
     MPDAPNPPKN QTYSYLGPAG TFTEAALAQV AEARGQIWRP VNNVGEAFAD VISGRSFAAM
     IAIENSVDGG VTATQDALAS VPNLRIIGEY LVPVNFVLVA RPGTTLADVR VVNAHPVAYG
     QCRNWLEKTL PSHGHLPSSS NVAAASALLD TTQADAAIAP PGIEKHHDLV VLASNIGDNP
     NAVTRFVLVG RTAELTAPTG ADKTSLIIEL PSDRSGALLE MLEQFATRGV NLSLIQSRPI
     GDSLGRYRFV VDADGHILDE RVADALLGLR RFSPKVIFLG SYPRADKRPI EFTSRYDDGI
     FIEARDWLRG LVGGEPAE
//
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