ID PHEA_MYCS2 Reviewed; 310 AA.
AC A0R643; I7GFR7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 01-MAY-2013, entry version 45.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=MSMEG_6418, MSMEI_6250;
OS Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through
RT orthology and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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.
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DR EMBL; CP000480; ABK72631.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42676.1; -; Genomic_DNA.
DR RefSeq; YP_006570971.1; NC_018289.1.
DR RefSeq; YP_890631.1; NC_008596.1.
DR ProteinModelPortal; A0R643; -.
DR STRING; 246196.MSMEG_6418; -.
DR EnsemblBacteria; ABK72631; ABK72631; MSMEG_6418.
DR GeneID; 13427580; -.
DR GeneID; 4534511; -.
DR KEGG; msg:MSMEI_6250; -.
DR KEGG; msm:MSMEG_6418; -.
DR PATRIC; 18085063; VBIMycSme59918_6244.
DR eggNOG; COG0077; -.
DR HOGENOM; HOG000018970; -.
DR KO; K04518; -.
DR OMA; CRKWLDA; -.
DR ProtClustDB; PRK11898; -.
DR BioCyc; MSME246196:GJ4Y-6417-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; FALSE_NEG.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
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;
KW Reference proteome.
FT CHAIN 1 310 Prephenate dehydratase.
FT /FTId=PRO_0000382039.
FT DOMAIN 3 190 Prephenate dehydratase.
FT DOMAIN 203 269 ACT.
FT SITE 183 183 Essential for activity (By similarity).
SQ SEQUENCE 310 AA; 32464 MW; 05E0E37D5F39C0B2 CRC64;
MPRIAYLGPE GTFTEAALLQ MVAKGMVPGP AEDAGGFTPV RTDSTPGALS AVREGRADYA
CVPIENSIDG TVLPTLDSLA AGSPLQIYAE LTLDVAFTIV VRPGHDGPVR TVAAFPVAAA
QVRHWLAANL RDAEVVPAHS NAAAAHDVAE GRADAGVSTR LAAERCGLDI MAADVVDEPN
ARTRFVLVGL PGTPPPATGA DRTAVVLRLV NEPGALVSAM TEFSIRDIDL TRIESRPTRT
ELGTYMFFLD CAGHIDDDPV AEALKALHRR CVDVRYLGSW PTESAAGAPP PRLDEATTWL
EGLRAGSGGA
//
