ID   KVDS_HERA2              Reviewed;         521 AA.
AC   A9AWD5;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=(+)-kolavenyl diphosphate synthase {ECO:0000303|PubMed:25694050};
DE            EC=5.5.1.29 {ECO:0000269|PubMed:25694050};
DE   AltName: Full=Class II cyclase {ECO:0000303|PubMed:25694050};
DE   AltName: Full=Diterpene cyclase {ECO:0000305|PubMed:25694050};
GN   OrderedLocusNames=Haur_2145 {ECO:0000312|EMBL:ABX04785.1};
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95 {ECO:0000312|Proteomes:UP000000787};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DOMAIN.
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RX   PubMed=25694050; DOI=10.1002/cbic.201402652;
RA   Nakano C., Oshima M., Kurashima N., Hoshino T.;
RT   "Identification of a new diterpene biosynthetic gene cluster that produces
RT   O-methylkolavelool in Herpetosiphon aurantiacus.";
RL   ChemBioChem 16:772-781(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of (+)-O-methylkolavelool.
CC       Catalyzes the conversion of geranylgeranyl diphosphate into (+)-
CC       kolavenyl diphosphate. {ECO:0000269|PubMed:25694050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-kolavenyl
CC         diphosphate; Xref=Rhea:RHEA:54676, ChEBI:CHEBI:58756,
CC         ChEBI:CHEBI:138311; EC=5.5.1.29;
CC         Evidence={ECO:0000269|PubMed:25694050};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:25694050};
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC       activity, presumably through binding to Mg(2+).
CC       {ECO:0000305|PubMed:25694050}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; CP000875; ABX04785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9AWD5; -.
DR   SMR; A9AWD5; -.
DR   STRING; 316274.Haur_2145; -.
DR   EnsemblBacteria; ABX04785; ABX04785; Haur_2145.
DR   KEGG; hau:Haur_2145; -.
DR   eggNOG; COG1657; Bacteria.
DR   HOGENOM; CLU_041269_0_0_0; -.
DR   BioCyc; HAUR316274:GHYA-2173-MON; -.
DR   BRENDA; 5.5.1.29; 2656.
DR   Proteomes; UP000000787; Chromosome.
DR   GO; GO:0106242; F:kolavenyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR032696; SQ_cyclase_C.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF00432; Prenyltrans; 1.
DR   Pfam; PF13243; SQHop_cyclase_C; 1.
DR   SUPFAM; SSF48239; SSF48239; 2.
PE   1: Evidence at protein level;
KW   Isomerase; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..521
FT                   /note="(+)-kolavenyl diphosphate synthase"
FT                   /id="PRO_0000443953"
FT   MOTIF           311..314
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000305|PubMed:25694050"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
SQ   SEQUENCE   521 AA;  58496 MW;  DE1EBE4662E3E4AF CRC64;
     MSLIVDILID DLRALIRDLG QNGGLMSPSV YDTSQALRLY PTPSEEHVWP AVNWLISQQQ
     SDGGWGNPSM PLSRAVPTLA AILALRRHCQ RRSTFDGLLE AKRFLRRQLE YWEKPLPDNL
     PVGMELLLPY MLEEAYREEH QDDIDDVPIK LRLNIPLAPY RELIALGEHK RSLIQQKKPR
     AGTAPVYSWE AWASHADPEL IDGSGGIGHS PAATAAWLFA ANHNPNLRNE IAGAENYLRQ
     ASLATSESAP CIMPTAWPIP RFEQSFSLYA LVTGGILDFP SIQDVLKPQI ADLHQALKPR
     GIGFSDDFMP DGDDTAAAVA VLIAAGYPVD LAILNQFERE PYFVAYHGEL QPSISLTARA
     VHALDLAGVD ISRWWKIFID AQKLDGSWSG DKWNTSWLYT TCHVLIALKN SPYKTAMKEA
     VAALQVHQHP DGGWGIINRS TTVETAYAVL ALQNLREAGL LDDDDIHMLQ RGYNWLCIHY
     RPFRMKEYQC WLNKEIYCPQ RIDRAYELSA MLAVTLGELK L