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Database: UniProt
Entry: G8LRZ6_9FLAO
LinkDB: G8LRZ6_9FLAO
Original site: G8LRZ6_9FLAO 
ID   G8LRZ6_9FLAO            Unreviewed;       359 AA.
AC   G8LRZ6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   11-DEC-2019, entry version 35.
DE   SubName: Full=Bifunctional putative phospho-2-dehydro-3-deoxyheptonate aldolase, chorismate mutase {ECO:0000313|EMBL:AEU09369.1};
DE            EC=2.5.1.54 {ECO:0000313|EMBL:AEU09369.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:AEU09369.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:AEU09369.1};
GN   Name=aroG {ECO:0000313|EMBL:AEU09369.1};
GN   Synonyms=pheA {ECO:0000313|EMBL:AEU09369.1};
GN   ORFNames=BLBCPU_324 {ECO:0000313|EMBL:AEU09369.1};
OS   Blattabacterium sp. (Cryptocercus punctulatus) str. Cpu.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=1075399 {ECO:0000313|EMBL:AEU09369.1, ECO:0000313|Proteomes:UP000007112};
RN   [1] {ECO:0000313|EMBL:AEU09369.1, ECO:0000313|Proteomes:UP000007112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cpu {ECO:0000313|EMBL:AEU09369.1,
RC   ECO:0000313|Proteomes:UP000007112};
RX   PubMed=22094859;
RA   Neef A., Latorre A., Pereto J., Silva F.J., Pignatelli M., Moya A.;
RT   "Genome economization in the endosymbiont of the wood roach Cryptocercus
RT   punctulatus due to drastic loss of amino acid synthesis capabilities.";
RL   Genome Biol. Evol. 3:1437-1448(2011).
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DR   EMBL; CP003015; AEU09369.1; -; Genomic_DNA.
DR   STRING; 1075399.BLBCPU_324; -.
DR   EnsemblBacteria; AEU09369; AEU09369; BLBCPU_324.
DR   KEGG; bcp:BLBCPU_324; -.
DR   eggNOG; ENOG4107RI0; Bacteria.
DR   eggNOG; COG2876; LUCA.
DR   KO; K04516; -.
DR   Proteomes; UP000007112; Chromosome.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000313|EMBL:AEU09369.1};
KW   Lyase {ECO:0000313|EMBL:AEU09369.1};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:AEU09369.1}.
FT   DOMAIN          270..359
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   COILED          269..289
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   359 AA;  41443 MW;  191600FDA5DF417A CRC64;
     MMEKNILNNS IDRSWIEKFD KPLVISGPCS AESEKQIKET AIRMDTSYVQ VFRAGIWKPR
     TKPNNFEGIG EVGLQWLKNV KKNTGLMVAT EVANAEHVKL ALSFDIDILW IGARSTASPF
     TVQEIADSLK GKEEKIILVK NPIHPDLELW IGALERLFSK GIKKLGVIHR GFYTYKTSKY
     RNQPNWNILL NFNSILPRIP IICDPSHICG NKKGILEISK IAFHFFRCEG LMIESHCDPD
     NAWSDAKQQI TPEKLLEMLK NLIYSNYDDE KYQNQLDSLR ILIDEIDENI ITLLAERMKI
     SKKLGILKKK YNIALLQKNR WEYILNKSIK LGKELGVSEE IIEEIFKILH KESINIQKY
//
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