ID A0A011VU76_RUMAL Unreviewed; 370 AA. AC A0A011VU76; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 11-DEC-2019, entry version 21. DE SubName: Full=Prephenate dehydratase {ECO:0000313|EMBL:EXM38821.1}; GN ORFNames=RASY3_10720 {ECO:0000313|EMBL:EXM38821.1}, RASY3_19410 GN {ECO:0000313|EMBL:EXM38350.1}; OS Ruminococcus albus SY3. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM38821.1, ECO:0000313|Proteomes:UP000021369}; RN [1] {ECO:0000313|EMBL:EXM38821.1, ECO:0000313|Proteomes:UP000021369} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SY3 {ECO:0000313|EMBL:EXM38821.1, RC ECO:0000313|Proteomes:UP000021369}; RA Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B., RA Bayer E.A.; RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by RT comparative genome-wide analysis of six Ruminococcal strains."; RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EXM38821.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JEOB01000004; EXM38350.1; -; Genomic_DNA. DR EMBL; JEOB01000003; EXM38821.1; -; Genomic_DNA. DR RefSeq; WP_037288024.1; NZ_JEOB01000004.1. DR EnsemblBacteria; EXM38350; EXM38350; RASY3_19410. DR EnsemblBacteria; EXM38821; EXM38821; RASY3_10720. DR PATRIC; fig|1341156.4.peg.2087; -. DR Proteomes; UP000021369; Unassembled WGS sequence. 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; IPR001086; Preph_deHydtase. 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 PROSITE; PS51671; ACT; 1. DR PROSITE; PS51168; CHORISMATE_MUT_2; 1. DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Reference proteome {ECO:0000313|Proteomes:UP000021369}. FT DOMAIN 1..86 FT /note="Chorismate mutase" FT /evidence="ECO:0000259|PROSITE:PS51168" FT DOMAIN 105..279 FT /note="Prephenate dehydratase" FT /evidence="ECO:0000259|PROSITE:PS51171" FT DOMAIN 291..370 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT COILED 3..23 FT /evidence="ECO:0000256|SAM:Coils" FT SITE 272 FT /note="Essential for prephenate dehydratase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2" SQ SEQUENCE 370 AA; 41665 MW; 5BC22D2615022C7C CRC64; MDLNDIRAEI NEVDKQLQEL FSKRMELCGK VADYKIANGL PVFQKDREKQ IIANVTEGAP EGLQGATRVY FQTMMDISKC LQYRKMFDNT GFIPFKKLDL SGRHRVAVPG TFGSYNHIAC SELFEDADTM FFDNFEEIFK AVSAGAAEFG ILPIINSTAG SVVQTYELMR QYDFKICAQA KLKISHCLAA RKGVRLEDIH DIYSHEQALR QCSDLINRGA YKAHSFSNTS LAACYVKEST EPCAAICSEK CAEDLGLEIL RRSVQNAAEN YTKFILISHE TFKADNADTI SVCLALPHQS SSLYRLLTKF SVAGLNMTMI ESMPIANTEF DVMFYLDFKG DIGKKEVTTL LSELSHELSY FKFLGNYKEV //