HUMS_ARATH
ID HUMS_ARATH Reviewed; 547 AA.
AC Q84UU4; Q84YI3; Q9FLW5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Alpha-humulene/(-)-(E)-beta-caryophyllene synthase;
DE EC=4.2.3.-;
DE AltName: Full=Terpenoid synthase 21;
DE Short=AtTPS21;
GN Name=TPS21; Synonyms=PUP8; OrderedLocusNames=At5g23960; ORFNames=MZF18.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12566586; DOI=10.1105/tpc.007989;
RA Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E., Gershenzon J.;
RT "Biosynthesis and emission of terpenoid volatiles from Arabidopsis
RT flowers.";
RL Plant Cell 15:481-494(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RX PubMed=12805595; DOI=10.1104/pp.102.017798;
RA Scutt C.P., Vinauger-Douard M., Fourquin C., Ailhas J., Kuno N., Uchida K.,
RA Gaude T., Furuya M., Dumas C.;
RT "The identification of candidate genes for a reverse genetic analysis of
RT development and function in the Arabidopsis gynoecium.";
RL Plant Physiol. 132:653-665(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
RA Aubourg S., Lecharny A., Bohlmann J.;
RT "Genomic analysis of the terpenoid synthase (AtTPS) gene family of
RT Arabidopsis thaliana.";
RL Mol. Genet. Genomics 267:730-745(2002).
RN [6]
RP GENE FAMILY.
RX PubMed=12777052; DOI=10.1023/a:1023005504702;
RA Lange B.M., Ghassemian M.;
RT "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT in isoprenoid and chlorophyll metabolism.";
RL Plant Mol. Biol. 51:925-948(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15918888; DOI=10.1111/j.1365-313x.2005.02417.x;
RA Tholl D., Chen F., Petri J., Gershenzon J., Pichersky E.;
RT "Two sesquiterpene synthases are responsible for the complex mixture of
RT sesquiterpenes emitted from Arabidopsis flowers.";
RL Plant J. 42:757-771(2005).
RN [8]
RP INDUCTION BY HERBIVORY.
RX PubMed=18400103; DOI=10.1186/1471-2164-9-154;
RA Ehlting J., Chowrira S.G., Mattheus N., Aeschliman D.S., Arimura G.,
RA Bohlmann J.;
RT "Comparative transcriptome analysis of Arabidopsis thaliana infested by
RT diamond back moth (Plutella xylostella) larvae reveals signatures of stress
RT response, secondary metabolism, and signalling.";
RL BMC Genomics 9:154-154(2008).
CC -!- FUNCTION: Involved in sesquiterpene (C15) biosynthesis. The major
CC products are beta-caryophyllene and alpha-humulene. Does not convert
CC geranyl diphosphate (GPP) to any monoterpenes.
CC {ECO:0000269|PubMed:12566586, ECO:0000269|PubMed:15918888}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for farnesyl diphosphate {ECO:0000269|PubMed:15918888};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84UU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84UU4-2; Sequence=VSP_041593;
CC -!- TISSUE SPECIFICITY: Expressed exclusively in flowers. Expressed in the
CC flower stigmata and also detected in the mesocarp cell layers of the
CC silique wall. {ECO:0000269|PubMed:12566586,
CC ECO:0000269|PubMed:12805595, ECO:0000269|PubMed:15918888}.
CC -!- INDUCTION: Induced in response to the caterpillar P.xylostella feeding.
CC {ECO:0000269|PubMed:18400103}.
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 -!- DISRUPTION PHENOTYPE: Does not emit (E)-beta-caryophyllene, alpha-
CC copaene and alpha-humulene. {ECO:0000269|PubMed:15918888}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08719.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF497491; AAO85539.1; -; mRNA.
DR EMBL; AJ544238; CAD66638.1; -; mRNA.
DR EMBL; AB009056; BAB08719.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93238.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93239.1; -; Genomic_DNA.
DR RefSeq; NP_001190374.1; NM_001203445.1. [Q84UU4-2]
DR RefSeq; NP_197784.2; NM_122301.4. [Q84UU4-1]
DR AlphaFoldDB; Q84UU4; -.
DR SMR; Q84UU4; -.
DR STRING; 3702.AT5G23960.1; -.
DR PaxDb; Q84UU4; -.
DR PRIDE; Q84UU4; -.
DR ProteomicsDB; 232122; -. [Q84UU4-1]
DR EnsemblPlants; AT5G23960.1; AT5G23960.1; AT5G23960. [Q84UU4-1]
DR EnsemblPlants; AT5G23960.2; AT5G23960.2; AT5G23960. [Q84UU4-2]
DR GeneID; 832461; -.
DR Gramene; AT5G23960.1; AT5G23960.1; AT5G23960. [Q84UU4-1]
DR Gramene; AT5G23960.2; AT5G23960.2; AT5G23960. [Q84UU4-2]
DR KEGG; ath:AT5G23960; -.
DR Araport; AT5G23960; -.
DR TAIR; locus:2178657; AT5G23960.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; Q84UU4; -.
DR OMA; IASCEFE; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q84UU4; -.
DR BioCyc; ARA:AT5G23960-MON; -.
DR BioCyc; MetaCyc:AT5G23960-MON; -.
DR BRENDA; 4.2.3.57; 399.
DR SABIO-RK; Q84UU4; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q84UU4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84UU4; baseline and differential.
DR Genevisible; Q84UU4; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IDA:TAIR.
DR GO; GO:0080017; F:alpha-humulene synthase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:TAIR.
DR GO; GO:0016106; P:sesquiterpenoid biosynthetic process; IDA:TAIR.
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 Alternative splicing; Cytoplasm; Lyase; Magnesium; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..547
FT /note="Alpha-humulene/(-)-(E)-beta-caryophyllene synthase"
FT /id="PRO_0000348421"
FT MOTIF 299..303
FT /note="DDXXD motif"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT VAR_SEQ 321..328
FT /note="WLPVVPDE -> YSICNI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12805595"
FT /id="VSP_041593"
FT CONFLICT 73
FT /note="Y -> C (in Ref. 1; AAO85539)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="A -> G (in Ref. 1; AAO85539)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="S -> N (in Ref. 1; AAO85539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 63619 MW; D9380654373B735D CRC64;
MGSEVNRPLA DFPANIWEDP LTSFSKSDLG TETFKEKHST LKEAVKEAFM SSKANPIENI
KFIDALCRLG VSYHFEKDIV EQLDKSFDCL DFPQMVRQEG CDLYTVGIIF QVFRQFGFKL
SADVFEKFKD ENGKFKGHLV TDAYGMLSLY EAAQWGTHGE DIIDEALAFS RSHLEEISSR
SSPHLAIRIK NALKHPYHKG ISRIETRQYI SYYEEEESCD PTLLEFAKID FNLLQILHRE
ELACVTRWHH EMEFKSKVTY TRHRITEAYL WSLGTYFEPQ YSQARVITTM ALILFTALDD
MYDAYGTMEE LELFTDAMDE WLPVVPDEIP IPDSMKFIYN VTVEFYDKLD EELEKEGRSG
CGFHLKKSLQ KTANGYMQEA KWLKKDYIAT FDEYKENAIL SSGYYALIAM TFVRMTDVAK
LDAFEWLSSH PKIRVASEII SRFTDDISSY EFEHKREHVA TGIDCYMQQF GVSKERAVEV
MGNIVSDAWK DLNQELMRPH VFPFPLLMRV LNLSRVIDVF YRYQDAYTNP KLLKEHIVSL
LIETIPI
