ID A0A2K9E0B8_9FIRM Unreviewed; 251 AA.
AC A0A2K9E0B8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN Name=uppS {ECO:0000313|EMBL:AUG57217.1};
GN ORFNames=B9R14_10860 {ECO:0000313|EMBL:PQQ67196.1}, HVS_06455
GN {ECO:0000313|EMBL:AUG57217.1};
OS Acetivibrio saccincola.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1677857 {ECO:0000313|EMBL:AUG57217.1, ECO:0000313|Proteomes:UP000233534};
RN [1] {ECO:0000313|EMBL:AUG57217.1, ECO:0000313|Proteomes:UP000233534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GGR1 {ECO:0000313|EMBL:AUG57217.1}, and SR1
RC {ECO:0000313|Proteomes:UP000233534};
RA Pechtl A., Ruckert C., Koeck D.E., Maus I., Winkler A., Kalinowski J.,
RA Puhler A., Schwarz W.W., Zverlov V.V., Schluter A., Liebl W.;
RT "Complete genome sequence of Herbivorax saccincola GGR1, a novel
RT Cellulosome-producing hydrolytic bacterium in a thermophilic biogas plant,
RT established by Illumina and Nanopore MinION sequencing.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PQQ67196.1, ECO:0000313|Proteomes:UP000239720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7 {ECO:0000313|EMBL:PQQ67196.1,
RC ECO:0000313|Proteomes:UP000239720};
RX PubMed=29482868; DOI=10.1016/j.syapm.2018.01.010;
RA Aikawa S., Baramee S., Sermsathanaswadi J., Thianheng P., Tachaapaikoon C.,
RA Shikata A., Waeonukul R., Pason P., Ratanakhanokchai K., Kosugi A.;
RT "Characterization and high-quality draft genome sequence of Herbivorax
RT saccincola A7, an anaerobic, alkaliphilic, thermophilic, cellulolytic, and
RT xylanolytic bacterium.";
RL Syst. Appl. Microbiol. 41:261-269(2018).
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|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01139}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000256|HAMAP-
CC Rule:MF_01139}.
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DR EMBL; CP025197; AUG57217.1; -; Genomic_DNA.
DR EMBL; NEMB01000003; PQQ67196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9E0B8; -.
DR KEGG; hsc:HVS_06455; -.
DR OrthoDB; 4191603at2; -.
DR Proteomes; UP000233534; Chromosome.
DR Proteomes; UP000239720; Unassembled WGS sequence.
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; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10291:SF48; DITRANS,POLYCIS-UNDECAPRENYL-DIPHOSPHATE SYNTHASE ((2E,6E)-FARNESYL-DIPHOSPHATE SPECIFIC); 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|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01139};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01139}; Reference proteome {ECO:0000313|Proteomes:UP000233534};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT ACT_SITE 31
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 79
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 32..35
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 76..78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 251 AA; 29044 MW; F537BC3E7F463A1E CRC64;
MSFIDRFFKK DKYINKLNKS KLPKHIAIIM DGNGRWAKRR GLPRTVGHRE GAKTLKTIST
FCGNIGIKYL TVYAFSTENW KRPKEEVDAL MDLLLDYLKN AEKHIGGKDV RIQTIGDISV
LSSEIQKEIE RVTRETKNNS GLILNIALNY GGRNEMVHCV KSIVEKIEKG EITKEDINEE
IISENLYTKD IPDPDILIRP GGESRLSNFL LWQAAYTEIW YTDVLWPDFR EKHIIDALLD
YQNRNRRFGG L
//
