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Database: UniProt
Entry: A0A1J4U7X0_9ARCH
LinkDB: A0A1J4U7X0_9ARCH
Original site: A0A1J4U7X0_9ARCH 
ID   A0A1J4U7X0_9ARCH        Unreviewed;       351 AA.
AC   A0A1J4U7X0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   11-DEC-2019, entry version 10.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OIO20748.1};
GN   ORFNames=AUJ17_05385 {ECO:0000313|EMBL:OIO20748.1};
OS   Candidatus Micrarchaeota archaeon CG1_02_47_40.
OC   Archaea; Candidatus Micrarchaeota.
OX   NCBI_TaxID=1805247 {ECO:0000313|EMBL:OIO20748.1, ECO:0000313|Proteomes:UP000183913};
RN   [1] {ECO:0000313|EMBL:OIO20748.1, ECO:0000313|Proteomes:UP000183913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_47_40 {ECO:0000313|EMBL:OIO20748.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIO20748.1}.
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DR   EMBL; MNVE01000016; OIO20748.1; -; Genomic_DNA.
DR   Proteomes; UP000183913; 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; PF01842; ACT; 1.
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; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}.
FT   DOMAIN          1..88
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   DOMAIN          88..260
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          272..349
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   COILED          4..24
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   351 AA;  39120 MW;  FCB16F81203A2000 CRC64;
     MENLEKERKK IDAIDAKVVS LLDERAKAAK EIGKKKSEAG KTEVIQTSRE REVIRKVSSR
     AKLLPKGDVA SIYTQIISAC RGLQKKVRVG YLGPEGTYSH IAALSYFGQN TELISHRTIS
     SAFASFEEGE VSLIIVPVEN SSGGSVGETL DNLYRANGYI VGELVLPIRH CLLAKKGVAH
     SRVKTIIAHP NALLQCSKFI ERNKFLTQDC ASTASACRKL DRQSASIGSE LAAELFSLEV
     LKRNIGDYED NTTRFIIVGR SPCQKTGKDK TSLLFTLPHK PGTLYQTLGV FAKEKINLLK
     VESRPYKGRK WEYLFFVDFE GHECEPKVER VLKKIRRISE SLRVLGSYPA E
//
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