ISPT_ZYMMO
ID ISPT_ZYMMO Reviewed; 248 AA.
AC Q9X5F1; Q5NND4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Isoprenyl transferase {ECO:0000255|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139};
GN Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=ZMO1152;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee H.J., Kang H.S.;
RT "Sequence analysis of 43D2 fosmid clone of Zymomonas mobilis ZM4.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC with allylic pyrophosphates generating different type of terpenoids.
CC {ECO:0000255|HAMAP-Rule:MF_01139}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01139};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_01139}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29658.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF124757; AAD29658.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE008692; AAV89776.2; -; Genomic_DNA.
DR RefSeq; WP_011240979.1; NZ_CP035711.1.
DR AlphaFoldDB; Q9X5F1; -.
DR SMR; Q9X5F1; -.
DR STRING; 264203.ZMO1152; -.
DR EnsemblBacteria; AAV89776; AAV89776; ZMO1152.
DR GeneID; 58026927; -.
DR KEGG; zmo:ZMO1152; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_1_5; -.
DR OMA; PRTEGHK; -.
DR OrthoDB; 1630604at2; -.
DR Proteomes; UP000001173; 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; -; 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 PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..248
FT /note="Isoprenyl transferase"
FT /id="PRO_0000123725"
FT ACT_SITE 28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 29..32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 73..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ SEQUENCE 248 AA; 27715 MW; 45EDC27E65E9773C CRC64;
MIAPLANSAV KPHKSASFVP RHVAIIMDGN GRWASARHLP RIAGHKKGAD AVKTTVRAAA
EMGIEVLTLY AFSSENWRRP ASEVADLMGL LRLCLRQEMH NIKERGICLK VIGDYTRLDQ
DLVALLNQAI EITANNTRLT LVFALNYGAQ DELVHVTKRI AEKAKEGQLD PENIDVGTIE
SLLYTHDLPP LDLVIRTSGE KRLSNFLLWQ AAYAELLFID TLWPDFGSET LKAAVEEYAR
RERRYGGL
