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Database: UniProt
Entry: B8J3L5_DESDA
LinkDB: B8J3L5_DESDA
Original site: B8J3L5_DESDA 
ID   B8J3L5_DESDA            Unreviewed;       419 AA.
AC   B8J3L5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   31-JUL-2019, entry version 52.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:ACL48250.1};
GN   OrderedLocusNames=Ddes_0336 {ECO:0000313|EMBL:ACL48250.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL48250.1, ECO:0000313|Proteomes:UP000002598};
RN   [1] {ECO:0000313|EMBL:ACL48250.1, ECO:0000313|Proteomes:UP000002598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 / DSM 6949 {ECO:0000313|Proteomes:UP000002598};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L.,
RA   Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans
RT   str. ATCC 27774.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001358; ACL48250.1; -; Genomic_DNA.
DR   STRING; 525146.Ddes_0336; -.
DR   EnsemblBacteria; ACL48250; ACL48250; Ddes_0336.
DR   KEGG; dds:Ddes_0336; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   HOGENOM; HOG000018971; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   BioCyc; DDES525146:G1GUN-345-MONOMER; -.
DR   Proteomes; UP000002598; Chromosome.
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   Pfam; PF01842; ACT; 1.
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; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002598}.
FT   DOMAIN       30    120       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      120    298       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      322    399       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1     25       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        291    291       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   419 AA;  45628 MW;  7A0CE60E6C3F31F7 CRC64;
     MGDSNSRWPG PASMPECGPE CGTGRKEKIH NADERLSTIR HEIDAVDQDL LDLFNRRAAL
     SREVGRIKAG SPGIIFRPVR EKEVLDSLAA RNPGPLPEDH LRAIWREIFS SSRALQRPQN
     VAYLGPEGTF SYFAGIEYLG HAATFHPCND IAQVFEEVAS GRCELGVVPL ENSLQGTVGV
     SFDLFLKHEV FIQAELFSRI SHCLLSNAPS LAAVRTVYSH PQPLAQCGTW LRTHLPNAGL
     VPVESTAAAA QRAAQGPDQE HAAAIGHGKL ADLMSLGTLA SRIEDEPGNW TRFVIIGPKV
     SAAQGGKLQN PQPGHGGADK TSLLFTLPDK AGALSRVLDL LAGHGINMRK LESRPMRGQC
     WKYVFFADVE SDLEDPRHAD LLVQLGHACT GFRILGSYPT GPQLDRLDLH TDEPEQKES
//
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