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Database: UniProt
Entry: G2FD29_9GAMM
LinkDB: G2FD29_9GAMM
Original site: G2FD29_9GAMM 
ID   G2FD29_9GAMM            Unreviewed;       365 AA.
AC   G2FD29;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   10-APR-2019, entry version 29.
DE   SubName: Full=Chorismate mutase I / prephenate dehydratase {ECO:0000313|EMBL:EGW55409.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:EGW55409.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:EGW55409.1};
GN   ORFNames=TevJSym_ad01430 {ECO:0000313|EMBL:EGW55409.1};
OS   endosymbiont of Tevnia jerichonana (vent Tica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria;
OC   sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW55409.1, ECO:0000313|Proteomes:UP000005167};
RN   [1] {ECO:0000313|EMBL:EGW55409.1, ECO:0000313|Proteomes:UP000005167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H.,
RA   Hecker M., Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and
RT   Tevnia jerichonana share an identical physiology as revealed by
RT   proteogenomic analyses.";
RL   ISME J. 0:0-0(2011).
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGW55409.1}.
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DR   EMBL; AFZB01000004; EGW55409.1; -; Genomic_DNA.
DR   RefSeq; WP_005963800.1; NZ_AFZB01000004.1.
DR   STRING; 1049564.TevJSym_ad01430; -.
DR   EnsemblBacteria; EGW55409; EGW55409; TevJSym_ad01430.
DR   PATRIC; fig|1049564.3.peg.813; -.
DR   BioCyc; EOF1049564:G10W2-818-MONOMER; -.
DR   Proteomes; UP000005167; 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; IPR010957; G/b/e-P-prot_chorismate_mutase.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
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; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005167};
KW   Isomerase {ECO:0000313|EMBL:EGW55409.1};
KW   Lyase {ECO:0000313|EMBL:EGW55409.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005167}.
FT   DOMAIN        5     97       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN       97    272       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      284    361       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED       11     38       {ECO:0000256|SAM:Coils}.
FT   SITE        265    265       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   365 AA;  39800 MW;  678B7969E394441F CRC64;
     MDEAVSDDQK LAAIRDRIDA IDEEIQRLFN ARAEAAQEVA RIKLAADPQA QFYRPEREAQ
     VLRRIKERNS GPLDPEEVAR LFREIMSACL ALEQPLQVAF LGPEGTFTQA AALKHFGHSV
     QCLPMGSIGD VFSEVESGAC HYGVVPVENS TEGVISHTLD SFVSSPLLIC GEVTLRINHH
     LLSSESGLQQ IRTVYSHQQS LAQCRGWLDR HLPQAERVAV GSNAEAARMA SQHAGVAAIA
     GETAAEIYGL PQLVSNIEDE AGNTTRFLVI GKKDAGASGD DKTSLLLSTQ NRAGGLHGLL
     SPFAEHSISM TRIESRPSRR GIWDYVFFVD INGHRSDPAV AEALRQLEQQ ASLFRVLGSY
     PKAVL
//
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