ID A0A132MMY9_9ACTN Unreviewed; 253 AA.
AC A0A132MMY9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN ORFNames=LI90_858 {ECO:0000313|EMBL:KWW99224.1}, TH66_04395
GN {ECO:0000313|EMBL:KWX05006.1}, TR74_19175
GN {ECO:0000313|EMBL:KWX07330.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99224.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|EMBL:KWX05006.1, ECO:0000313|Proteomes:UP000070659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBT1 {ECO:0000313|EMBL:KWX05006.1,
RC ECO:0000313|Proteomes:UP000070659};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000070598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBT1 {ECO:0000313|Proteomes:UP000070598};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KWW99224.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:KWW99224.1};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Woodward J., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) 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. Z-FPP synthase
CC subfamily. {ECO:0000256|ARBA:ARBA00038453}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01139}.
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:KWW99224.1}.
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DR EMBL; LAXD01000001; KWW99224.1; -; Genomic_DNA.
DR EMBL; JYIJ01000013; KWX05006.1; -; Genomic_DNA.
DR EMBL; JYIK01001062; KWX07330.1; -; Genomic_DNA.
DR RefSeq; WP_066884378.1; NZ_LAXD01000001.1.
DR AlphaFoldDB; A0A132MMY9; -.
DR STRING; 1469144.LI90_858; -.
DR PATRIC; fig|1469144.10.peg.973; -.
DR OrthoDB; 4191603at2; -.
DR Proteomes; UP000070188; Unassembled WGS sequence.
DR Proteomes; UP000070598; Unassembled WGS sequence.
DR Proteomes; UP000070659; 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: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:UP000070188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT ACT_SITE 33
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 34..37
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 50
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 78..80
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 253 AA; 28932 MW; 9C8C246EB1F89A16 CRC64;
MGLRDLLYRV YERRLQSSLN PQQIPRHVGV ILDGNRRWAR SYAKRITEGH KAGADKIHEL
LDWCDEVGVE VVTLWLLSTD NLNRPRDELA ALFEIIEGVV RDLMAAGRWR VHPVGALDLL
PDSTARLLKE ADEATRDVPG LVVNAAIGYG GRREIADAVR SLLYEHASRG TSIEELAEIL
DVEHIAEHLY TRGQPDPDLL IRTSGEQRLS GFLLWQSAHS EFYFCEAYWP DFRKVDFLRA
LRSYAARQRR YGV
//
