ID D1PTX6_9BACT Unreviewed; 255 AA.
AC D1PTX6;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:EFA45184.1};
GN ORFNames=HMPREF0645_0411 {ECO:0000313|EMBL:EFA45184.1};
OS Hallella bergensis DSM 17361.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hallella.
OX NCBI_TaxID=585502 {ECO:0000313|EMBL:EFA45184.1, ECO:0000313|Proteomes:UP000003160};
RN [1] {ECO:0000313|EMBL:EFA45184.1, ECO:0000313|Proteomes:UP000003160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17361 {ECO:0000313|EMBL:EFA45184.1,
RC ECO:0000313|Proteomes:UP000003160};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (OCT-2009) 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}.
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:EFA45184.1}.
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DR EMBL; ACKS01000020; EFA45184.1; -; Genomic_DNA.
DR RefSeq; WP_007174760.1; NZ_GG704782.1.
DR AlphaFoldDB; D1PTX6; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_1_10; -.
DR OrthoDB; 4191603at2; -.
DR Proteomes; UP000003160; 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:UP000003160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT REGION 231..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 18
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 19..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 63..65
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 190..192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 255 AA; 29571 MW; DF3A9779399C1375 CRC64;
MAEPDMTKIP RHIAIIMDGN GRWAAEQGKE RSFGHQAGVD TVRCITSECT RLGVKFLTLY
TFSTENWSRP QDEISALMGL VLTSLEDEIF MKNNVRFRVV GEMERLPKDV QDKLKETMDH
TAKNSAMTMV VALSYSSRWE ITKATREIAE EVKAGKLRPE DINEDIVNEH MATNFMPDPD
LLIRTGGDLR ISNYMLWQIA YSELYFCDTY WPAFREKDLH RAIVSYQNRQ RRFGKTEEQV
EQESGVKQET EKEKE
//
