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Database: UniProt
Entry: K0NG66_DESTT
LinkDB: K0NG66_DESTT
Original site: K0NG66_DESTT 
ID   K0NG66_DESTT            Unreviewed;       367 AA.
AC   K0NG66;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-FEB-2019, entry version 29.
DE   SubName: Full=PheA: P-protein {ECO:0000313|EMBL:CCK80156.1};
GN   Name=pheA {ECO:0000313|EMBL:CCK80156.1};
GN   OrderedLocusNames=TOL2_C19950 {ECO:0000313|EMBL:CCK80156.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK80156.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK80156.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica To12 marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-1355(2013).
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DR   EMBL; FO203503; CCK80156.1; -; Genomic_DNA.
DR   RefSeq; WP_014957489.1; NC_018645.1.
DR   EnsemblBacteria; CCK80156; CCK80156; TOL2_C19950.
DR   KEGG; dto:TOL2_C19950; -.
DR   PATRIC; fig|651182.5.peg.2374; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; DTOL651182:G1HBZ-2155-MONOMER; -.
DR   Proteomes; UP000007347; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:InterPro.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR010958; Chorismate_mutase_highGC-bac.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01808; CM_M_hiGC-arch; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007347};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT   DOMAIN        4     94       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN       94    269       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      281    358       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED        3     30       {ECO:0000256|SAM:Coils}.
FT   SITE        262    262       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   367 AA;  41669 MW;  96A9C6C1E4D76934 CRC64;
     MNEKNSEHEL NRLRNQIDTI DSQLLSLINQ RLEIGQKVGT IKKQTGSQIL DRTRERKLIE
     RLFKLNRGPA GKDLLRYVFN VIITATREIQ KPKTISFLGP EASYTHVAAL THFKHSGKFV
     EQPNLYEIFR EVEKNQSHFG VVPVENSIEG AVNHTLDLFA DFDLNICAEH YEPVSHDLLS
     ITGEAEDVQK IYSHPQALAQ CKTWIKKKFA HAEIFETTST SKAALLASDD KTIAAIAGKQ
     AAHLYELQSI ESKIEDYSGN ITRFLVIGKE MPEPTGQDKT SIMFATSHVP GALFKALEPV
     NRAQLNMLKL ESRPTRHHNW SYYFFLDIEG HKLDKRVADT IEEIKQYSLS LKILGSYPVF
     AKEAHEA
//
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