GCAS_CHIPD
ID GCAS_CHIPD Reviewed; 321 AA.
AC C7PLV2;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=(-)-gamma-cadinene synthase ((2Z,6E)-farnesyl diphosphate cyclizing) {ECO:0000303|PubMed:23307484};
DE EC=4.2.3.62 {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:27666571, ECO:0000269|PubMed:27829890};
DE AltName: Full=Terpene cyclase {ECO:0000303|PubMed:23307484};
DE AltName: Full=Type I terpene cyclase {ECO:0000303|PubMed:23307484};
GN OrderedLocusNames=Cpin_4730 {ECO:0000312|EMBL:ACU62166.1};
OS Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / LMG 13176 / NBRC
OS 15968 / NCIMB 11800 / UQM 2034).
OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=485918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM
RC 2034 {ECO:0000312|Proteomes:UP000002215};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Sims D., Meinche L., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Chitinophaga pinensis DSM 2588.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM
RC 2034;
RX PubMed=23307484; DOI=10.1002/anie.201209103;
RA Rabe P., Dickschat J.S.;
RT "Rapid chemical characterization of bacterial terpene synthases.";
RL Angew. Chem. Int. Ed. 52:1810-1812(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RC STRAIN=ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM
RC 2034;
RX PubMed=27666571; DOI=10.1002/anie.201608042;
RA Rinkel J., Rabe P., Garbeva P., Dickschat J.S.;
RT "Lessons from 1,3-hydride shifts in sesquiterpene cyclizations.";
RL Angew. Chem. Int. Ed. 55:13593-13596(2016).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN, AND PATHWAY.
RC STRAIN=ATCC 43595 / DSM 2588 / LMG 13176 / NBRC 15968 / NCIMB 11800 / UQM
RC 2034;
RX PubMed=27829890; DOI=10.3762/bjoc.12.173;
RA Rabe P., Schmitz T., Dickschat J.S.;
RT "Mechanistic investigations on six bacterial terpene cyclases.";
RL Beilstein J. Org. Chem. 12:1839-1850(2016).
CC -!- FUNCTION: Catalyzes the conversion of (2Z,6E)-farnesyl diphosphate
CC (FPP) to yield the bicyclic sesquiterpene (1S,6S,7R)-(-)-gamma-cadinene
CC via a 1,10-cyclization, which requires the abstraction of the
CC pyrophosphate from FPP to yield a germacradienyl cation
CC (PubMed:23307484, PubMed:27666571, PubMed:27829890). The only accepted
CC substrate is (2Z,6E)-farnesyl diphosphate (FPP) (PubMed:27829890).
CC {ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:27666571,
CC ECO:0000269|PubMed:27829890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6E)-farnesyl diphosphate = (-)-gamma-cadinene +
CC diphosphate; Xref=Rhea:RHEA:28639, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:63203, ChEBI:CHEBI:162247; EC=4.2.3.62;
CC Evidence={ECO:0000269|PubMed:23307484, ECO:0000269|PubMed:27666571,
CC ECO:0000269|PubMed:27829890};
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|PubMed:27829890}.
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:27829890}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; CP001699; ACU62166.1; -; Genomic_DNA.
DR RefSeq; WP_012792334.1; NC_013132.1.
DR AlphaFoldDB; C7PLV2; -.
DR SMR; C7PLV2; -.
DR STRING; 485918.Cpin_4730; -.
DR EnsemblBacteria; ACU62166; ACU62166; Cpin_4730.
DR KEGG; cpi:Cpin_4730; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_042538_4_2_10; -.
DR OMA; DLIEYAM; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000002215; 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.
FT CHAIN 1..321
FT /note="(-)-gamma-cadinene synthase ((2Z,6E)-farnesyl
FT diphosphate cyclizing)"
FT /id="PRO_0000443242"
FT MOTIF 82..86
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:27829890"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 309..310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 79
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 83
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 155
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 178
FT /note="Plays a critical role for abstraction of the
FT pyrophosphate group"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 321 AA; 37087 MW; F276B8B8A93AB54D CRC64;
MPTITLPRII YPFPSLINQF VTAAHEQNRQ WVADFGFITT PEAMARFDRS RFAWLAARAF
PHAGFHELCT IANFNTWLFM LDDQCDEAQL GKKAVYLEHV TDGFMNILKH NTPVDTVLGR
SFTDIWERMQ ALGDTAWQTR FIRSMEEYFT SCHWEAGNRA ADIVPTVAEY VTMRPYTGAL
FADVEAIEII EKVYLPAHIL QHFIVQRLVL ACNNIVCWAN DIFSCAKEAR QGDVHNLVLV
LQHERNSTLQ EAVNETARMH NEEVKLFTAL EKLLPSFGAE MDRELERFMA VLRSWITANY
DWSYHDTGRY QVKEVEVVIN S
