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Database: UniProt
Entry: A0A1X0GH90_9MYCO
LinkDB: A0A1X0GH90_9MYCO
Original site: A0A1X0GH90_9MYCO 
ID   A0A1X0GH90_9MYCO        Unreviewed;       292 AA.
AC   A0A1X0GH90;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   31-JUL-2019, entry version 12.
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=BST36_29495 {ECO:0000313|EMBL:ORB13416.1};
OS   Mycolicibacterium moriokaense.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=39691 {ECO:0000313|EMBL:ORB13416.1, ECO:0000313|Proteomes:UP000192354};
RN   [1] {ECO:0000313|EMBL:ORB13416.1, ECO:0000313|Proteomes:UP000192354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP105393 {ECO:0000313|EMBL:ORB13416.1,
RC   ECO:0000313|Proteomes:UP000192354};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ORB13416.1}.
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DR   EMBL; MVIB01000052; ORB13416.1; -; Genomic_DNA.
DR   BioCyc; GCF_002086395:BST36_RS29475-MONOMER; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000192354; 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; 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:UP000192354};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254}.
FT   DOMAIN        3    184       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      198    273       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION      272    292       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        177    177       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   292 AA;  30595 MW;  EEAF1CDFBF53ECED CRC64;
     MTGIAYLGPE GTFTEAALHG MVEAQLVPVT DFEWIPATST AAALEMVRSG DAAYACVPIE
     NSIEGSILPT LDSLATGSPL QIFAEYTLDI AFTIAVRKGA TDPATIAAFP VARAQVAKWA
     AKSLPNAEFV AADSNAAAAI DVANGRADAA VTTPLAAERH GLEVLATGVV DERNARTRFV
     LVGPVGPPPA RTDSDRTSVV LRLDNVPGAL AAALSEFAIR DIGLTRIESR PTRTELGTYI
     FFLDCEGHVD DPPVAEALKA LVERSADVRF LGSWPMGSDE PPRSGQAGEE NP
//
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