ID A0A3N1QIB3_9MICO Unreviewed; 276 AA.
AC A0A3N1QIB3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN ORFNames=EDF46_2155 {ECO:0000313|EMBL:ROQ38517.1};
OS Frondihabitans sp. PhB188.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=2485200 {ECO:0000313|EMBL:ROQ38517.1, ECO:0000313|Proteomes:UP000269803};
RN [1] {ECO:0000313|EMBL:ROQ38517.1, ECO:0000313|Proteomes:UP000269803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PhB188 {ECO:0000313|EMBL:ROQ38517.1,
RC ECO:0000313|Proteomes:UP000269803};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (NOV-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. 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:ROQ38517.1}.
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DR EMBL; RJUO01000003; ROQ38517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1QIB3; -.
DR Proteomes; UP000269803; 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:SF43; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE COMPLEX SUBUNIT DHDDS; 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:UP000269803};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT ACT_SITE 54
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 55..58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 59
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 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 231..233
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 276 AA; 30881 MW; 4161BABC49879123 CRC64;
MGYRSFVTTR RRTTGGDAGE NPVGRGFAYR LYQRRIRRGL AGLELPHHVA MIVDGNRRWA
KQRMLETAAH GHRAGAAKIR EFLTWCDELG IKVVTLYLLS ADNLTNRHDA ELEALVDIIS
ELAHDLSRTG DWRVQHVGAV DGLPGSLVDA LHDAESRTAD HTGLHVNLAV GYGGRREIAD
AMRSIVRAHG EGGGTIDDLA EVLTPELIAD HLYTGGQPDP DLVIRTSGEQ RLSDFMLWQS
AHSEFYFVEA FYPDLREVDF LRAVRDFANR HRRYGS
//