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Database: UniProt
Entry: A0A345GZ05_9FLAO
LinkDB: A0A345GZ05_9FLAO
Original site: A0A345GZ05_9FLAO 
ID   A0A345GZ05_9FLAO        Unreviewed;       246 AA.
AC   A0A345GZ05;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN   Name=ispU {ECO:0000313|EMBL:AXG69543.1};
GN   ORFNames=KORDIASMS9_01766 {ECO:0000313|EMBL:AXG69543.1};
OS   Kordia sp. SMS9.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=2282170 {ECO:0000313|EMBL:AXG69543.1, ECO:0000313|Proteomes:UP000253780};
RN   [1] {ECO:0000313|EMBL:AXG69543.1, ECO:0000313|Proteomes:UP000253780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS9 {ECO:0000313|EMBL:AXG69543.1,
RC   ECO:0000313|Proteomes:UP000253780};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Clarke A.K.,
RA   Godhe A.;
RT   "Genome Sequence of Kordia sp. Strain SMS9 Isolated from a Culture of the
RT   Diatom Skeletonema marinoi.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC       with allylic pyrophosphates generating different type of terpenoids.
CC       {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01139}.
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DR   EMBL; CP031153; AXG69543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345GZ05; -.
DR   KEGG; kos:KORDIASMS9_01766; -.
DR   OrthoDB; 4191603at2; -.
DR   Proteomes; UP000253780; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; Decaprenyl diphosphate synthase-like; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR018520; UPP_synth-like_CS.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   NCBIfam; TIGR00055; uppS; 1.
DR   PANTHER; PTHR10291:SF0; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE 2; 1.
DR   PANTHER; PTHR10291; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253780};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01139}.
FT   ACT_SITE        21
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         21
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         22..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         66..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         195..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT   BINDING         208
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   246 AA;  28443 MW;  9FE393CBDD67A2A3 CRC64;
     MSLAEKIQKA FLPRHLAIIM DGNGRWAKQK GKLRVFGHEN GTKSVREIVE ASAELGIKNL
     TLYAFSTENW NRPKLEVDAL MRLLVSSLKK ELKVLQKNNI KLQAIGCLDT LPKKANRELF
     EVIEKTKNNT HMTLTLALSY GSREELKNAV KEICQKVKNN IISLESIDES IINQHLYTHD
     LPDVDLLIRT SGEHRISNFL LWQIAYAELY FTNILWPDFS KEDLYEALIN YQNRERRFGK
     TSEQIN
//
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