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Database: UniProt
Entry: G7MC95_9CLOT
LinkDB: G7MC95_9CLOT
Original site: G7MC95_9CLOT 
ID   G7MC95_9CLOT            Unreviewed;       377 AA.
AC   G7MC95;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   11-DEC-2019, entry version 29.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:EHI97770.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:EHI97770.1};
GN   ORFNames=CDLVIII_1067 {ECO:0000313|EMBL:EHI97770.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHI97770.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHI97770.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHI97770.1};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-13(2013).
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DR   EMBL; CM001240; EHI97770.1; -; Genomic_DNA.
DR   RefSeq; WP_009168452.1; NZ_CM001240.1.
DR   STRING; 641107.CDLVIII_1067; -.
DR   EnsemblBacteria; EHI97770; EHI97770; CDLVIII_1067.
DR   BioCyc; CSP641107:G10TE-1106-MONOMER; -.
DR   Proteomes; UP000005106; Chromosome.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
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; IPR011279; Chorismate_mutase_GmP.
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; TIGR01805; CM_mono_grmpos; 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}; Lyase {ECO:0000313|EMBL:EHI97770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT   DOMAIN          1..88
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          108..285
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          297..377
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   COILED          4..24
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   SITE            278
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   377 AA;  43536 MW;  330B4BC3837AD22D CRC64;
     MTELDDYRKS IDEIDKKITE LFEKRMDVVL KVGEYKKNNN LAVFDESREK EVIEKNLGYL
     KNKNYEEGTR EFFTQIMEIA KKLENKKIEK AVGEYKFTQR QSSINKKKIG YYGVKGSFTE
     EAMMKYFGDI KAAKAYEEFE NVFAAVKDGE IDYGVVPIEN SSTGAISQVY DLLYKYGFYI
     VGEECIKINQ HLIGVKDTKL ETIKEVYSHP QGFEQSTEFL KKHNDWKLIP FHSTADSVKL
     VSDLNDKSKV AIASKRAASI YNLEIIKENI NNQSENSTRF IIISKELETN SSCNKVSVVF
     SLEHKAGTLY KLLSHFAEND INMMKIESRP MEKGAWKYFL YVDFEGNLES EKVRKALSLI
     EQSSAYFKLI GGYKKYS
//
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