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Database: UniProt
Entry: A0A1M4WG32_9BACT
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Original site: A0A1M4WG32_9BACT 
ID   A0A1M4WG32_9BACT        Unreviewed;       383 AA.
AC   A0A1M4WG32;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 10.
DE   SubName: Full=Chorismate mutase /prephenate dehydratase {ECO:0000313|EMBL:SHE80208.1};
GN   ORFNames=SAMN05443144_103211 {ECO:0000313|EMBL:SHE80208.1};
OS   Aliifodinibius roseus.
OC   Bacteria; Balneolaeota; Balneolia; Balneolales; Balneolaceae;
OC   Aliifodinibius.
OX   NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHE80208.1, ECO:0000313|Proteomes:UP000184041};
RN   [1] {ECO:0000313|EMBL:SHE80208.1, ECO:0000313|Proteomes:UP000184041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21986 {ECO:0000313|EMBL:SHE80208.1,
RC   ECO:0000313|Proteomes:UP000184041};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQUS01000003; SHE80208.1; -; Genomic_DNA.
DR   RefSeq; WP_073059793.1; NZ_FQUS01000003.1.
DR   BioCyc; GCF_900129315:BUB16_RS04165-MONOMER; -.
DR   Proteomes; UP000184041; 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   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   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:UP000184041};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184041}.
FT   DOMAIN        1     90       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      104    284       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      298    375       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED        5     32       {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      82     82       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      86     86       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        277    277       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   383 AA;  43246 MW;  B9189F1CDB18260C CRC64;
     MADKLDQIRQ QLDETDKQII DALAKRQQLV REVSSFKIDE KKNIRDLQRE EQLLDKITKL
     AREAGLDRYF AEQLFKDIID HSVRFQTHTL VDHQNVRNDA QQVRVAYQGT EGAYSDQAAA
     RHFEERYTEV HSIGYDTFRQ AARAVEEGEA DYAILPIENT TAGSISDTYD ILGDGKLHIV
     GEEALRIIHC LLAVEEVPVD KIRRILSHPQ AIAQCSNFLA KQHRCKIESY IDTAMAAKKV
     LEDGDLSQAA IAGAHAAEIY DLKILKRDLA NQPENFTRFV VVSTDPVEID RQIPCKTSLL
     MVTSHDKGAL VSCLNIIAEH DIGMTKLESR PKPNEPWKYQ FYLDIEGNIA EPDTRLALEE
     LEQKASSLKI LGSYPAQVGN GDH
//
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