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Database: UniProt
Entry: A0A1H2Q349_9FIRM
LinkDB: A0A1H2Q349_9FIRM
Original site: A0A1H2Q349_9FIRM 
ID   A0A1H2Q349_9FIRM        Unreviewed;       377 AA.
AC   A0A1H2Q349;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 7.
DE   SubName: Full=Chorismate mutase / prephenate dehydratase {ECO:0000313|EMBL:SDW01626.1};
GN   ORFNames=SAMN05216391_10195 {ECO:0000313|EMBL:SDW01626.1};
OS   Lachnospiraceae bacterium KHCPX20.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=1855375 {ECO:0000313|EMBL:SDW01626.1, ECO:0000313|Proteomes:UP000199590};
RN   [1] {ECO:0000313|EMBL:SDW01626.1, ECO:0000313|Proteomes:UP000199590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHCPX20 {ECO:0000313|EMBL:SDW01626.1,
RC   ECO:0000313|Proteomes:UP000199590};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNOC01000001; SDW01626.1; -; Genomic_DNA.
DR   Proteomes; UP000199590; 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   Complete proteome {ECO:0000313|Proteomes:UP000199590};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199590}.
FT   DOMAIN        1     88       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      111    289       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      301    376       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   BINDING       8      8       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      25     25       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      36     36       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      45     45       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      49     49       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      80     80       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      84     84       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        282    282       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   377 AA;  43230 MW;  703BDE643655EC26 CRC64;
     MRDLKDIRVE IDAIDDQLLT LYHQRLLLAH NVAEYKIANH RPVLDKKREE EKLEVLTAKV
     SNSFEKEGIR ELFELIMSTS RKRQYQMMRE HGVTVNHNYK PVEAFDFSDA HIVYQGVEGA
     YSQVAMEKFF GHGVHSTHVA TWKDAMEALK EKKADYAVLP IENSTAGAVT QIYDLLSSYD
     VSIIGEEIIK IEHALLALPG TRLSDIKRVY SHPQALMQCD HFLQETLPEV EAHSVLNTAL
     SAQKIHDEGK KDQAAIAGAI NARIYNLEIL QSSIQDEESN ETRFFVVSRN RTFRNNAKQI
     SICFELPNEE GSLYRILSHF TFNSINMNRI ESRPLEGRPW EYRFFVDFEG NLQDDGVTNA
     LIGLAEETRN LRILGNY
//
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