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Database: UniProt
Entry: D0YW15_PHODD
LinkDB: D0YW15_PHODD
Original site: D0YW15_PHODD 
ID   D0YW15_PHODD            Unreviewed;       390 AA.
AC   D0YW15;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   16-JAN-2019, entry version 34.
DE   SubName: Full=Chorismate mutase I/prephenate dehydratase {ECO:0000313|EMBL:EEZ40295.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:EEZ40295.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:EEZ40295.1};
GN   ORFNames=VDA_001320 {ECO:0000313|EMBL:EEZ40295.1};
OS   Photobacterium damselae subsp. damselae CIP 102761.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ40295.1, ECO:0000313|Proteomes:UP000003579};
RN   [1] {ECO:0000313|EMBL:EEZ40295.1, ECO:0000313|Proteomes:UP000003579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ40295.1,
RC   ECO:0000313|Proteomes:UP000003579};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA   Bartels D.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; ADBS01000001; EEZ40295.1; -; Genomic_DNA.
DR   RefSeq; WP_005297856.1; NZ_ADBS01000001.1.
DR   STRING; 675817.VDA_001320; -.
DR   EnsemblBacteria; EEZ40295; EEZ40295; VDA_001320.
DR   GeneID; 34511756; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   OrthoDB; 1280729at2; -.
DR   BioCyc; PDAM675817:G11UI-182-MONOMER; -.
DR   Proteomes; UP000003579; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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: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; IPR010952; CM_P_1.
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; TIGR01797; CM_P_1; 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:UP000003579};
KW   Isomerase {ECO:0000313|EMBL:EEZ40295.1};
KW   Lyase {ECO:0000313|EMBL:EEZ40295.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003579}.
FT   DOMAIN        2     93       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      107    287       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      301    378       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED        8     35       {ECO:0000256|SAM:Coils}.
FT   BINDING      12     12       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      29     29       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      40     40       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      49     49       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      53     53       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      85     85       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      89     89       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        280    280       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   390 AA;  43824 MW;  48076958188DA945 CRC64;
     MTEPTYSLDE IRLRVSQIDN QLLELLAQRR QLSLEVAKSK ISTAKPVRDK AREHDLLLKL
     IETGKEKQLD PQYVTQLFHT IIEDSVLYQQ AFLQQLINPE NAQPSARIAF LGSKGSYSHL
     ASLNYFSRKQ TQLLEMSCSS FRDVINEVEL GHADYGVLPI ENTSSGSINE VYDLLQHTSL
     SIVGEITQPI EHCLLTAVET QLEAIDTLYS HPQPHQQCSE FVHQLGEIKQ EYCSSTADAM
     KIVAELSQPN IAAIGNATSG EMYGLYSLTE HIANQEQNFT RFIVVARKAI DVTPLIPAKT
     TFIMSTGQSA GSLVECLLIL KNHNINMAKL ESRPVMGNPW EEMFYVDVEE NIKSEVMQQA
     MEELSQVTRF IKVLGCYATE NVKPTEVTID
//
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