PRISS_STRE2
ID PRISS_STRE2 Reviewed; 372 AA.
AC B5H7H3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Pristinol synthase {ECO:0000303|PubMed:27403888};
DE EC=4.2.3.182 {ECO:0000269|PubMed:27403888};
DE AltName: Full=Terpene synthase {ECO:0000303|PubMed:27403888};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:27403888};
GN ORFNames=SSDG_01120 {ECO:0000312|EMBL:EDY62784.1};
OS Streptomyces pristinaespiralis (strain ATCC 25486 / DSM 40338 / CBS 914.69
OS / JCM 4507 / NBRC 13074 / NRRL 2958 / 5647).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=457429;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 / NRRL
RC 2958 / 5647 {ECO:0000312|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25486 / DSM 40338 / CBS 914.69 / JCM 4507 / NBRC 13074 / NRRL
RC 2958 / 5647 {ECO:0000312|EMBL:EDY62784.1,
RC ECO:0000312|Proteomes:UP000002805};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces pristinaespiralis strain ATCC 25486.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND SUBSTRATE SPECIFICITY.
RX PubMed=27403888; DOI=10.1002/anie.201605425;
RA Klapschinski T.A., Rabe P., Dickschat J.S.;
RT "Pristinol, a sesquiterpene alcohol with an unusual skeleton from
RT Streptomyces pristinaespiralis.";
RL Angew. Chem. Int. Ed. 55:10141-10144(2016).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) to yield a new 5-8 bicyclic (pristinane) sesquiterpenol (+)-
CC (2S,3R,9R)-pristinol via a 1,11-cyclization, which requires the
CC abstraction of the pyrophosphate from FPP to yield the humulyl cation.
CC The only accepted substrate is farnesyl diphosphate (FPP).
CC {ECO:0000269|PubMed:27403888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-(2S,3R,9R)-pristinol
CC + diphosphate; Xref=Rhea:RHEA:54372, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138165, ChEBI:CHEBI:175763;
CC EC=4.2.3.182; Evidence={ECO:0000269|PubMed:27403888};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5HDJ6};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp (DDXXD) motif is important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305|PubMed:27403888}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CM000950; EDY62784.1; -; Genomic_DNA.
DR RefSeq; WP_005320742.1; NZ_CM000950.1.
DR AlphaFoldDB; B5H7H3; -.
DR SMR; B5H7H3; -.
DR STRING; 457429.ABJI02000741_gene345; -.
DR EnsemblBacteria; EDY62784; EDY62784; SSDG_01120.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_0_11; -.
DR OMA; EWLLSMA; -.
DR BRENDA; 4.2.3.182; 12737.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000002805; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..372
FT /note="Pristinol synthase"
FT /id="PRO_0000443323"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..104
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:27403888"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 337..338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 372 AA; 41393 MW; 9A24F6895CC65C55 CRC64;
MAHETTSGRR LPDPTSPSDP TRRTAAIRIP FPARLNPHAE RARQHTLQWV QETGLLTGDE
ATAEYDTLRL ERLMAYFYPD ASAGDLELAA DFNAWFFIFD DQFDGGLGTR PHEIRGVVDA
LVGTMTTDGA PRPADVRDTP LVRAFRDIWL RSTAGAPYAW RLRFRDHWQA YLAAHVGEAH
HRNADRLPSL EQFLEVRRHS IGVQPCLDFT ERCGGYALPD ELYRSFPLRE MREITGDVVI
FVNDIVSLVK ELAAGDINNS VVIEREHKGC TLEESVEHIT ALANARTARF ARLAASLPGT
LADLGVPAPS REHVSHYVDG MRHVMAGNLS WSLATSRYDE TGIAAVSGGR RRPWDGLTTA
TGTASPRHPR RA
