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Database: UniProt
Entry: R7A662_9FIRM
LinkDB: R7A662_9FIRM
Original site: R7A662_9FIRM 
ID   R7A662_9FIRM            Unreviewed;       360 AA.
AC   R7A662;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   13-FEB-2019, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CDD50974.1};
GN   ORFNames=BN599_01240 {ECO:0000313|EMBL:CDD50974.1};
OS   Firmicutes bacterium CAG:308.
OC   Bacteria; Firmicutes; environmental samples.
OX   NCBI_TaxID=1263016 {ECO:0000313|EMBL:CDD50974.1, ECO:0000313|Proteomes:UP000017945};
RN   [1] {ECO:0000313|EMBL:CDD50974.1, ECO:0000313|Proteomes:UP000017945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:308 {ECO:0000313|Proteomes:UP000017945};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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:CDD50974.1}.
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DR   EMBL; CBHE010000063; CDD50974.1; -; Genomic_DNA.
DR   Proteomes; UP000017945; 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; IPR011279; Chorismate_mutase_GmP.
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   TIGRFAMs; TIGR01805; CM_mono_grmpos; 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   Complete proteome {ECO:0000313|Proteomes:UP000017945};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017945}.
FT   DOMAIN        1     88       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN       92    267       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      277    354       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED        4     24       {ECO:0000256|SAM:Coils}.
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        260    260       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   360 AA;  40764 MW;  B28091B64BECB9E1 CRC64;
     MNQIEKARLE IDSVDKEIAR LYEKRLDAVK EVLEYKKANA LPILDAGRED AIIEKNQKYI
     QNKEYVDSYI DFMKKVMSNS RDFQQTLLSS DVVAYAGVKG AFSQIVASRM FPAEKKLNYT
     NFEDVFKAVV NKDAQYGIIP FENTNSGLVG EVLDALLEYP VYIQQVVDQR VEQCLLGVEN
     ATLKDVEWVY SKDQALAQSK VFLKGLNVQT VAYPNTAMAA QYVASQNDVR KAAIGAKENA
     DLYGLKILAE NIEENISNTT RFIVIGLEPQ TQGNRFSVCL IVKHQSGALA RIIETIAQHG
     LNMQSIQSRP IKNRPFEYFF FIEMDGNLEM KNTRECLKDI KKVTQSVKYL GTYSLKGKDD
//
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