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TPSGD_VITVI
ID   TPSGD_VITVI             Reviewed;         557 AA.
AC   Q6Q3H3; A5BPP0; A5C4C3; E0CT34;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=(-)-germacrene D synthase;
DE            EC=4.2.3.22;
DE            EC=4.2.3.75;
GN   OrderedLocusNames=VIT_19s0014g04930;
GN   ORFNames=VIT_00014569001, VITISV_013313, VITISV_030783, Vv19s0014g04930;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=cv. Gewuerztraminer;
RX   PubMed=15464152; DOI=10.1016/j.phytochem.2004.08.017;
RA   Lucker J., Bowen P., Bohlmann J.;
RT   "Vitis vinifera terpenoid cyclases: functional identification of two
RT   sesquiterpene synthase cDNAs encoding (+)-valencene synthase and (-)-
RT   germacrene D synthase and expression of mono- and sesquiterpene synthases
RT   in grapevine flowers and berries.";
RL   Phytochemistry 65:2649-2659(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Gewuerztraminer;
RA   Steinmetz A.A., Lommele A., Drescher B., Driesel A.J.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024;
RX   PubMed=17721507; DOI=10.1038/nature06148;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir;
RX   PubMed=18094749; DOI=10.1371/journal.pone.0001326;
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "A high quality draft consensus sequence of the genome of a heterozygous
RT   grapevine variety.";
RL   PLoS ONE 2:E1326-E1326(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of germacrene D. Can use
CC       farnesyl diphosphate as substrate, but not geranyl diphosphate or
CC       geranylgeranyl diphosphate. Produces mainly (-)-germacrene D along with
CC       gamma-cadinene. {ECO:0000269|PubMed:15464152}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-
CC         1(10),5-dien-11-ol + diphosphate; Xref=Rhea:RHEA:22436,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:46734,
CC         ChEBI:CHEBI:175763; EC=4.2.3.22;
CC         Evidence={ECO:0000269|PubMed:15464152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate;
CC         Xref=Rhea:RHEA:12016, ChEBI:CHEBI:33019, ChEBI:CHEBI:49044,
CC         ChEBI:CHEBI:175763; EC=4.2.3.75;
CC         Evidence={ECO:0000269|PubMed:15464152};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers. Detected in stems, young
CC       leaves and tendrils.
CC   -!- DEVELOPMENTAL STAGE: Expressed in flower buds and detected in open pre-
CC       anthesis flowers, flowers after anthesis and in early stages of fruit
CC       onset.
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}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY561842; AAS66357.1; -; mRNA.
DR   EMBL; FN595229; CBI20483.3; -; Genomic_DNA.
DR   EMBL; FN597046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AM481907; CAN68620.1; -; Genomic_DNA.
DR   EMBL; AM466733; CAN83470.1; -; Genomic_DNA.
DR   RefSeq; NP_001268213.1; NM_001281284.1.
DR   AlphaFoldDB; Q6Q3H3; -.
DR   SMR; Q6Q3H3; -.
DR   STRING; 29760.VIT_19s0014g04930.t01; -.
DR   PRIDE; Q6Q3H3; -.
DR   GeneID; 100232954; -.
DR   KEGG; vvi:100232954; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   HOGENOM; CLU_003125_7_2_1; -.
DR   InParanoid; Q6Q3H3; -.
DR   OrthoDB; 360509at2759; -.
DR   BRENDA; 4.2.3.75; 6671.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000009183; Chromosome 19.
DR   ExpressionAtlas; Q6Q3H3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034004; F:germacradienol synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052577; F:germacrene-D 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   Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..557
FT                   /note="(-)-germacrene D synthase"
FT                   /id="PRO_0000412252"
FT   MOTIF           310..314
FT                   /note="DDXXD motif"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        7
FT                   /note="G -> V (in Ref. 3; CBI20483 and 4; CAN68620/
FT                   CAN83470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="H -> Y (in Ref. 4; CAN68620/CAN83470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="F -> L (in Ref. 4; CAN83470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="S -> T (in Ref. 4; CAN83470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="F -> S (in Ref. 3; CBI20483 and 4; CAN68620/
FT                   CAN83470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="P -> H (in Ref. 3; CBI20483 and 4; CAN68620/
FT                   CAN83470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        491..496
FT                   /note="PQPVRE -> HKQVRD (in Ref. 3; CBI20483 and 4;
FT                   CAN68620/CAN83470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539..541
FT                   /note="FGA -> SGT (in Ref. 3; CBI20483 and 4; CAN68620/
FT                   CAN83470)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   557 AA;  64269 MW;  BE6F4E1965265928 CRC64;
     MSVQSSGVLL APSKNLSPEV GRRCANFHPS IWGDHFLSYA SEFTNTDDHL KQHVQQLKEE
     VRKMLMAADD DSAQKLLLID AIQRLGVAYH FESEIDEVLK HMFDGSVVSA EEDVYTASLR
     FRLLRQQGYH VSCDLFNNFK DNEGNFKESL SSDVRGMLSL YEATHFRVHG EDILDEALAF
     TTTHLQSATK HSSNPLAEQV VHALKQPIRK GLPRLEARHY FSVYQADDSH NKALLKLAKL
     DFNLLQKLHQ KELSDISAWW KDLDFAHKLP FARDRVVECY FWILGVYFEP QFFFARRILT
     KVIAMTSIID DIYDVYGTLE ELELFTEAVE RWDISAIDQL PEYMRVCYQA LLYVYSEIEE
     EMAKEGRSYR LYYAKEAMKN QVRAYYEEAK WLQVQQIPTM EEYMPVALVT SAYSMLATTS
     FVGMGDAVTK ESFDWIFSKP KIVRASAIVC RLMDDMVFHK FEQKRGHVAS AVECYMKQHG
     ASEQETPNEF PQPVREAWKD INEECLIPTA VPMPILMRVL NLARVIDVIY KNEDGYTHFG
     AVLKDFVTSM LIDPVPI
 
 
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