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Database: UniProt
Entry: A0A1X6XNI2_9MICO
LinkDB: A0A1X6XNI2_9MICO
Original site: A0A1X6XNI2_9MICO 
ID   A0A1X6XNI2_9MICO        Unreviewed;       337 AA.
AC   A0A1X6XNI2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-FEB-2019, entry version 7.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|RuleBase:RU361254};
DE            Short=PDT {ECO:0000256|RuleBase:RU361254};
DE            EC=4.2.1.51 {ECO:0000256|RuleBase:RU361254};
GN   Name=pheA {ECO:0000256|RuleBase:RU361254};
GN   ORFNames=FM105_13655 {ECO:0000313|EMBL:SLN00831.1};
OS   Brevibacterium yomogidense.
OC   Bacteria; Actinobacteria; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=946573 {ECO:0000313|EMBL:SLN00831.1, ECO:0000313|Proteomes:UP000196581};
RN   [1] {ECO:0000313|EMBL:SLN00831.1, ECO:0000313|Proteomes:UP000196581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B Co 03.10 {ECO:0000313|EMBL:SLN00831.1,
RC   ECO:0000313|Proteomes:UP000196581};
RA   Peterson S.W.;
RL   Submitted (FEB-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;
CC         EC=4.2.1.51; Evidence={ECO:0000256|RuleBase:RU361254};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|RuleBase:RU361254}.
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DR   EMBL; FWFF01000020; SLN00831.1; -; Genomic_DNA.
DR   BioCyc; GCF_900163715:FM105_RS13495-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000196581; 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   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Complete proteome {ECO:0000313|Proteomes:UP000196581};
KW   Lyase {ECO:0000256|RuleBase:RU361254, ECO:0000313|EMBL:SLN00831.1};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196581}.
FT   DOMAIN        8    207       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      222    299       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        200    200       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   337 AA;  35588 MW;  50D9387B8474F6DB CRC64;
     MTDQSSTRYA YLGPAATFTE AALIGLLTER GVLETAERIP MRSADAMLEA VRAGEVDAAV
     VPIENSVEGG VPATLDALTR YGRLQIVAEA VVPVRFVLAA LPGTVTRETL RSYGTHPHAE
     AQTRLWMQRN APQAEYRVTS STAAAAQELA ASAEPAGASA GAAGSTDLPY QAVIGPLLAA
     QTYGLEVLAD DIGDNTLAET RFICVERPGA IPEPTGWDRT TIVVGLASDR AGALLEMLEQ
     LSARGVNMSR IESRPTGDGL GLYQFSIDVL GHVAEARVAE ALRGIHRVAG SVKFLGSYPM
     ASATRTELNG TKKAVDPRVA DDAFDRAQAW LDDVTGR
//
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