ID PHEA_MYCGI Reviewed; 309 AA.
AC A4T6G3;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 01-MAY-2013, entry version 41.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=Mflv_1145;
OS Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens
OS (strain ATCC 700033 / PYR-GCK)).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: Prephenate = phenylpyruvate + H(2)O + CO(2).
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Contains 1 ACT domain.
CC -!- SIMILARITY: Contains 1 prephenate dehydratase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000656; ABP43627.1; -; Genomic_DNA.
DR RefSeq; YP_001132415.1; NC_009338.1.
DR STRING; 350054.Mflv_1145; -.
DR EnsemblBacteria; ABP43627; ABP43627; Mflv_1145.
DR GeneID; 4972471; -.
DR KEGG; mgi:Mflv_1145; -.
DR PATRIC; 18030316; VBIMycGil17082_1170.
DR eggNOG; COG0077; -.
DR HOGENOM; HOG000018970; -.
DR KO; K04518; -.
DR OMA; CRKWLDA; -.
DR ProtClustDB; PRK11898; -.
DR BioCyc; MGIL350054:GHK8-1542-MONOMER; -.
DR UniPathway; UPA00121; UER00345.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; ISS:UniProtKB.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF00800; PDT; 1.
DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; FALSE_NEG.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Lyase; Phenylalanine biosynthesis.
FT CHAIN 1 309 Prephenate dehydratase.
FT /FTId=PRO_0000382034.
FT DOMAIN 3 191 Prephenate dehydratase.
FT DOMAIN 204 270 ACT.
FT SITE 184 184 Essential for activity (By similarity).
SQ SEQUENCE 309 AA; 32171 MW; 4E6E0668B4E3FEE6 CRC64;
MPGIAYLGPE GTFTEAALRA LDAQGLIPAT QSGAGSVTPL ATDSTPAALA AVRAGDADFA
CVPIENSIDG PVIPTLDSLA DGVPLQIYAE LTLDVSFTIA VRPGVTAADV RTVAAFPVAA
AQVKRWLSEN LPNVELVPSN SNAAAARDVA DGRAEAAVST ALATERYGLD TLAAGIVDEP
NARTRFVLVG CPGPPPKRTG SDRTSVVLRL DNVPGALVTA MNELAIRGID LTGIESRPTR
TELGTYRFYL DFVGHIDDDA VAGALRALHR RCADVRYLGS WPTGETGGAA PPPLDEATAW
LQRLREGRP
//
