(data stored in ACNUC10821 zone)

SWISSPROT: C8U2A5_ECO10

ID   C8U2A5_ECO10            Unreviewed;       299 AA.
AC   C8U2A5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   SubName: Full=Geranyltranstransferase {ECO:0000313|EMBL:BAI29263.1};
GN   Name=ispA {ECO:0000313|EMBL:BAI29263.1};
GN   OrderedLocusNames=ECO103_0395 {ECO:0000313|EMBL:BAI29263.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29263.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29263.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC       {ECO:0000256|RuleBase:RU004466}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010958; BAI29263.1; -; Genomic_DNA.
DR   RefSeq; WP_000347235.1; NC_013353.1.
DR   EnsemblBacteria; BAI29263; BAI29263; ECO103_0395.
DR   KEGG; eoh:ECO103_0395; -.
DR   HOGENOM; HOG000009101; -.
DR   KO; K00795; -.
DR   OMA; CEGQALD; -.
DR   BioCyc; ECOL585395:ECO103_RS02070-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2A5.
DR   SWISS-2DPAGE; C8U2A5.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Transferase {ECO:0000256|RuleBase:RU004466,
KW   ECO:0000313|EMBL:BAI29263.1}.
FT   COILED      253    280       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   299 AA;  32159 MW;  1801B576B441A248 CRC64;
     MDFPQQLEAC VKQANQALSR FIAPLPFQNT PVVETMQYGA LLGGKRLRPF LVYATGHMFG
     VSTNTLDAPA AAVECIHAYS LIHDDLPAMD DDDLRRGLPT CHVKFGEANA ILAGDALQTL
     AFSILSDANM PEVSDRDRIS MISELASASG IAGMCGGQAL DLDAEGKHVP LDALERIHRH
     KTGALIRAAV RLGALSAGDK GRRALPVLDK YAESIGLAFQ VQDDILDVVG DTATLGKRQG
     ADQQLGKSTY PALLGLEQAR KKARDLIDDA RQSLKQLAEQ SLDTSALEAL ADYIIQRNK
//

If you have problems or comments...

PBIL Back to PBIL home page