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Database: UniProt
Entry: A0A1A2KDV2_9MYCO
LinkDB: A0A1A2KDV2_9MYCO
Original site: A0A1A2KDV2_9MYCO 
ID   A0A1A2KDV2_9MYCO        Unreviewed;       313 AA.
AC   A0A1A2KDV2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-FEB-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=A5700_21180 {ECO:0000313|EMBL:OBG76778.1};
OS   Mycobacterium sp. E1214.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834123 {ECO:0000313|EMBL:OBG76778.1, ECO:0000313|Proteomes:UP000092248};
RN   [1] {ECO:0000313|EMBL:OBG76778.1, ECO:0000313|Proteomes:UP000092248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E1214 {ECO:0000313|EMBL:OBG76778.1,
RC   ECO:0000313|Proteomes:UP000092248};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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:OBG76778.1}.
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DR   EMBL; LZJC01000056; OBG76778.1; -; Genomic_DNA.
DR   RefSeq; WP_068204581.1; NZ_LZJC01000056.1.
DR   EnsemblBacteria; OBG76778; OBG76778; A5700_21180.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000092248; 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:UP000092248};
KW   Lyase {ECO:0000256|RuleBase:RU361254};
KW   Phenylalanine biosynthesis {ECO:0000256|RuleBase:RU361254}.
FT   DOMAIN        3    187       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      201    278       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        180    180       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   313 AA;  32655 MW;  7E8D598ACA3E862C CRC64;
     MTRIAYLGPE GTFTEAALRQ IIAAGLVPKH GVPDPLPTDS TAAALDAVRN GDADYACVPI
     ENSIDGSVTP TLDSLSIGSP LQVFAETTLD VAFSIVVAPG RGAAEVRTLA AFSVAAAQVR
     HWVAEHLPDA KLRAASSNAD AARQVAEGLA DAAVTSPLAA TRWGLPALAD GVVDEPNACT
     RFLLAGLPAP PPARTGADRT SVVLHIDNAP GALLGALTEF GIRGIDLTRI ESRPTRIALG
     TYVFFVDCVG HIDDDAVAEA LKALHRRCAD VRYLGSWPTG TPAGVQPPPA DEALRWLTRL
     REGKPEAAER SES
//
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