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Database: UniProt
Entry: A0A0M9E7A2_9DELT
LinkDB: A0A0M9E7A2_9DELT
Original site: A0A0M9E7A2_9DELT 
ID   A0A0M9E7A2_9DELT        Unreviewed;       368 AA.
AC   A0A0M9E7A2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   13-FEB-2019, entry version 10.
DE   SubName: Full=Bifunctional P-protein, chorismate mutase/prephenate dehydratase {ECO:0000313|EMBL:KPA15780.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:KPA15780.1};
GN   ORFNames=MHK_004014 {ECO:0000313|EMBL:KPA15780.1};
OS   Candidatus Magnetomorum sp. HK-1.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Candidatus Magnetomorum.
OX   NCBI_TaxID=1509431 {ECO:0000313|EMBL:KPA15780.1, ECO:0000313|Proteomes:UP000037988};
RN   [1] {ECO:0000313|Proteomes:UP000037988}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25079475; DOI=10.1111/1758-2229.12198;
RA   Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT   "Single-cell genomics reveals potential for magnetite and greigite
RT   biomineralization in an uncultivated multicellular magnetotactic
RT   prokaryote.";
RL   Environ. Microbiol. Rep. 6:524-531(2014).
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:KPA15780.1}.
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DR   EMBL; JPDT01001067; KPA15780.1; -; Genomic_DNA.
DR   EnsemblBacteria; KPA15780; KPA15780; MHK_004014.
DR   Proteomes; UP000037988; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
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; PS00858; PREPHENATE_DEHYDR_2; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000037988};
KW   Isomerase {ECO:0000313|EMBL:KPA15780.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037988}.
FT   DOMAIN        7     97       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN       97    272       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      284    361       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   SITE        265    265       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   368 AA;  41721 MW;  E905850B0116EBA7 CRC64;
     MKPDSTSDTD NPLIPCRDKI DEIDKKILSL LVDRQDMAYK VGQIKKEMGL GVFNMAREEQ
     VFRHLKSKSR GNLNPEAIHH IFSEIISAAR AVQQPIDVAY LGPEATFSHQ AAIYLYGKST
     TFRAAETIED VFSFVEKGMC QHGIVPIENS YEGSVNVTMD LFYKYDLKIC AEIFLRIRHH
     LLSKSDSMEP VECIYSHPMP FAQCRSWLRS NYPHVPTQKV ESTSTAAIIA QKNPKAAAIG
     SRLAAMTYKL NMLSENIEDQ PDNVTRFLIV SRNHAESTGK DKTSLLFFLN HKPGALYSAL
     KPLSDHNINM TRIESRPMKV RNWEYLFFAD IEGHISEPHV QSALKEMETH CAILKHLGSY
     PEGGMVWD
//
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