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Database: UniProt
Entry: A0A0Q5DQ95_9BURK
LinkDB: A0A0Q5DQ95_9BURK
Original site: A0A0Q5DQ95_9BURK 
ID   A0A0Q5DQ95_9BURK        Unreviewed;       357 AA.
AC   A0A0Q5DQ95;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   11-DEC-2019, entry version 24.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:KQQ46402.1};
GN   ORFNames=ASF61_18605 {ECO:0000313|EMBL:KQQ46402.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Duganella; unclassified Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ46402.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|Proteomes:UP000051032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|Proteomes:UP000051032};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|Proteomes:UP000051032};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQQ46402.1}.
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DR   EMBL; LMNW01000002; KQQ46402.1; -; Genomic_DNA.
DR   RefSeq; WP_056151547.1; NZ_LMNW01000002.1.
DR   EnsemblBacteria; KQQ46402; KQQ46402; ASF61_18605.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase.
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; TIGR01807; CM_P2; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
FT   DOMAIN          1..89
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          89..264
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          276..353
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            257
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   357 AA;  38581 MW;  CE6542F7070B14F5 CRC64;
     MNDKLKPLRE QIDAIDAQIL DLLNRRARVA QEVGHVKAET NAPVFRPERE AQVLRGVADR
     NPGPMGNAEM QTIFREIMSA CRALEKRVTV AFLGPAGTYS EQAVYQQFGT AVDVLACASI
     DEVFRATEAG TADFGVVPVE NSTEGAIGRT LDLLLNTPLT ISGEVAIAVR HSLLTGTGTM
     DGVTAICAHA QALAQCQIWL NNNYPEIERR AVSSNAEAAR MARDDHSVAA IAGERAGVRY
     SLGTVKANIQ DDPHNRTRFA VIGTLRTGPS GIDRTSMALA APHKAGSVYR LLGSLAQNGV
     SMTRFESRPA RNGNWEYYFY VDVEGHIENP AVARALEELQ GNAAFFKVLG SYPVSLT
//
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