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Database: UniProt
Entry: A0A1V3KA20_9PAST
LinkDB: A0A1V3KA20_9PAST
Original site: A0A1V3KA20_9PAST 
ID   A0A1V3KA20_9PAST        Unreviewed;       385 AA.
AC   A0A1V3KA20;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   12-SEP-2018, entry version 8.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:OOF70229.1};
GN   ORFNames=BKG89_04350 {ECO:0000313|EMBL:OOF70229.1};
OS   Rodentibacter heylii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1906744 {ECO:0000313|EMBL:OOF70229.1, ECO:0000313|Proteomes:UP000188820};
RN   [1] {ECO:0000313|EMBL:OOF70229.1, ECO:0000313|Proteomes:UP000188820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1998236014 {ECO:0000313|EMBL:OOF70229.1,
RC   ECO:0000313|Proteomes:UP000188820};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OOF70229.1}.
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DR   EMBL; MLAA01000014; OOF70229.1; -; Genomic_DNA.
DR   Proteomes; UP000188820; Unassembled WGS sequence.
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; 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; 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:UP000188820};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188820}.
FT   DOMAIN        1     92       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      105    285       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      299    376       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED        5     25       {ECO:0000256|SAM:Coils}.
FT   COILED       44     64       {ECO:0000256|SAM:Coils}.
FT   BINDING       9      9       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      26     26       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      37     37       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      46     46       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      50     50       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      84     84       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      88     88       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        278    278       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   385 AA;  44119 MW;  CD733CF4C5EF72AB CRC64;
     MALDLMEIRQ QITQIDRNLL KLLSERHRLA FDVARSKEIS KKPLRDLERE QQLLQELVRF
     AENENYQLEP QYITSVFQKI IEDSVLTQQV YLQKKLNERR EQSVHIAFLG KRGSYSHLAA
     RNYATRYQEQ LVELSCTSFD QVFETVQNGD ADFGVLPLEN TTSGAINEVY DLLQYTELSL
     VGEIAYPIKH CVLVNGGENI RKIQTLYSHP QVIQQCSKFI RSLEPVHIEY CESSSHAMQL
     VASLNKPNIA ALGNEDGGKL YGLSVLQENI ANQENNITRF IVIAKQPREV SPQIHTKTLL
     LMSTTQKAGA LVDALLVFKK YGINMTKLES RPIYGKPWEE MFYLEIEANI HHSDSWQALQ
     ELKEYSTTLK ILGCYPSEIV KPAKL
//
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