STS1_HUMLU
ID STS1_HUMLU Reviewed; 563 AA.
AC B6SCF5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Alpha-humulene synthase {ECO:0000305};
DE EC=4.2.3.104 {ECO:0000269|PubMed:18775972};
DE AltName: Full=Sesquiterpene synthase STS1 {ECO:0000303|PubMed:18775972};
DE Short=HlSTS1 {ECO:0000303|PubMed:18775972};
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486 {ECO:0000312|EMBL:ACI32639.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND PATHWAY.
RC TISSUE=Lupulin gland;
RX PubMed=18775972; DOI=10.1104/pp.108.125187;
RA Wang G., Tian L., Aziz N., Broun P., Dai X., He J., King A., Zhao P.X.,
RA Dixon R.A.;
RT "Terpene biosynthesis in glandular trichomes of hop.";
RL Plant Physiol. 148:1254-1266(2008).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of alpha-
CC humulene. Can use farnesyl diphosphate (FPP) as substrate, but not
CC geranyl diphosphate (GPP) or geranylgeranyl diphosphate (GGPP).
CC {ECO:0000269|PubMed:18775972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.104;
CC Evidence={ECO:0000269|PubMed:18775972};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:18775972};
CC -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:18775972}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:18775972}.
CC -!- TISSUE SPECIFICITY: Expressed in trichomes, cones and young leaves.
CC {ECO:0000269|PubMed:18775972}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; EU760350; ACI32639.1; -; mRNA.
DR AlphaFoldDB; B6SCF5; -.
DR SMR; B6SCF5; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0080017; F:alpha-humulene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..563
FT /note="Alpha-humulene synthase"
FT /id="PRO_0000439238"
FT MOTIF 316..320
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 563 AA; 66219 MW; 1C7652C3CAEAA087 CRC64;
MSTQILASSS QNEKIHKILR PTKKFQPPVW GERFLHYNIS EQELRYKQQQ VEELKEVVKK
EIFGESAYDV SHQLKLINVV ERLGLSYHFE SEIENELESI YNKSVGQNYI LKDENLHDAS
LRFRLLRQHG FRVSSPDIFE KFKDEDGNFK ECLVSDTIGL LSLYEASHLS CVGENILDEA
LAFTTTHLTE FLANKKEHDD PLSREISQAL ERPLRKSLER LAARHFISIY ENETSHNKVL
LQLAKLDFNL LQSIHKKELS EISRWWKESD FVLKFPFARE RIVELYLWIL GAYYEPQYSM
ARNVLTKIIA FASLADDIYD EYGTFEELEL LTEAVERWDI YIIDKLNPEY LQTFYKELLN
SYEEFEQELP KEETYRVHYA KERFKELLRS YLEEAWWLKE ERVPSFDEYL KISLISCGYH
MLIVSSLIGM KSSIVTKEVF EWLSMDRKII RASSTICRFM DDLAEHKFEQ EKNDEPTAVE
CYMKQYGVSE EEAYDELNKQ IANAWKEINE ELLKPTGVAS PILVRVLNFS KFMDLFYKNG
DSYTQVGKVA KDSVAALLID PIP
