AHUMS_PICGL
ID AHUMS_PICGL Reviewed; 575 AA.
AC F2XF97;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Alpha-humulene synthase {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.104 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Hum {ECO:0000303|PubMed:21385377};
DE Short=PgTPS-Hum {ECO:0000303|PubMed:21385377};
GN Name=TPS-Hum {ECO:0000303|PubMed:21385377};
OS Picea glauca (White spruce) (Pinus glauca).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3330;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. PG29;
RX PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA Dullat H.K., Bohlmann J.;
RT "Transcriptome mining, functional characterization, and phylogeny of a
RT large terpene synthase gene family in spruce (Picea spp.).";
RL BMC Plant Biol. 11:43-43(2011).
CC -!- FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of
CC sesquiterpene natural products included in conifer oleoresin secretions
CC and volatile emissions; these compounds contribute to biotic and
CC abiotic stress defense against herbivores and pathogens
CC (PubMed:21385377). Catalyzes the conversion of (2E,6E)-farnesyl
CC diphosphate (FPP) to (1E,4E,8E)-alpha-humulene (PubMed:21385377).
CC {ECO:0000269|PubMed:21385377}.
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:21385377};
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 -!- PATHWAY: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:21385377}.
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
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:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ426155; ADZ45513.1; -; mRNA.
DR UniPathway; UPA00924; -.
DR GO; GO:0080017; F:alpha-humulene synthase activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016106; P:sesquiterpenoid biosynthetic process; IDA:UniProtKB.
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..575
FT /note="Alpha-humulene synthase"
FT /id="PRO_0000454417"
FT MOTIF 325..329
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 575 AA; 66334 MW; 643D335F6069F02F CRC64;
MAQISESAAI PRRTANHHGN VWDDDLILSL DSPYGAPAYY ERLAKLIEEM KHLLLREMED
SNHDLIRRLQ IVDTLECLGI DRHFQHEIKT AALHYVYRCW NEKGIGMGSS DSGSKDLDAT
ALGLRALRLH RYNVSSGVLE NFQDENGKFF CNLTGDKRVR SMLSLLRASE ISFPGEKVMQ
EAKAFTREYL TQVLAGSGDV TDVDQSLLRE VKYALEFPWY CSAPRWEAKS FIEIYGQNQS
WLKSNINQEV LELAKLDFSI LQCIHQKEIQ CITRWWRDSE IAQLNFYRRR HVELYFWAVT
CIFEPEFSPS RIAFAKITTV GAVLDDLYDT HGTLDELKTI TEAVRRWDLS LIDDLPNNIK
IACQFFFNTA NELAVEVVKK QGRDMTALLK ATWQRYVESY LQEAEWIETR HVPSFNEYIK
NALVSSGMCI VNLIPLLLLG QLLANNIVEQ ILSPSKIQEL SELTIRLIDD IRDFEDEKER
GEIASIVECY MKDNPDSTLE NALNHIKGIL HVSLEELNWE FMKDDSVPLC CKKFTFNIVR
GLQFLYKYGD GISISNKEVK DQIFKILVDQ IPIED
