ID A0A0P1M534_9BACT Unreviewed; 272 AA.
AC A0A0P1M534; A0A0P1LEK0; A0A0P1LM21; A0A0P1LWP1; A0A0P1M5A3; A0A0P1M682;
AC A0A0P1MQB0; A0A0S4MPX5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
GN ORFNames=JGI4_00183 {ECO:0000313|EMBL:CUU01086.1};
OS Candidatus Kryptonium thompsoni.
OC Bacteria; Candidatus Kryptonia; Kryptonium.
OX NCBI_TaxID=1633631 {ECO:0000313|EMBL:CUU01086.1, ECO:0000313|Proteomes:UP000182011};
RN [1] {ECO:0000313|EMBL:CUU01086.1, ECO:0000313|Proteomes:UP000182011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JGI-4 {ECO:0000313|EMBL:CUU01086.1};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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|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; FAOP01000001; CUU01086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1M534; -.
DR STRING; 1633631.GCA_001442925_00183; -.
DR Proteomes; UP000182011; 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:UP000182011};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT ACT_SITE 39
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 40..43
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 52
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 84..86
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 213..215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 272 AA; 31589 MW; 7A5F23703135C718 CRC64;
MGDAVSSSKT EVKGYRDRKI QEELKSRGEI PKHIAIIMDG NGRWAKKRGL PRVAGHREGI
KSVRDVVEAC AQLGVKYLTL FAFSTENWKR PKYEVDTLMK LLIKVLRTEV DKLQKNDIKL
MAIGDIESLP VEVQRELKEA IEKTRNNKRM VLNLAISYSG RWEIIEAVKS IARDVKNGKV
KVDEIDDKLF SNYLKTAGMP EPDLLIRTSG EYRISNFLLW QIAYTELYIC DCLWPDFRRK
HLYEAIKDYQ RRERRFGMTS EQIKKKSFNG NA
//
