ID   GERAS_NOSP7             Reviewed;         323 AA.
AC   B2J4A4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Germacrene A synthase;
DE            EC=4.2.3.90;
DE   AltName: Full=5-epi-alpha-selinene synthase;
DE   AltName: Full=8a-epi-alpha-selinene synthase;
DE   AltName: Full=Terpene synthase;
GN   OrderedLocusNames=Npun_R3832;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION AS A GERMACRENE A SYNTHASE, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18658271; DOI=10.1128/jb.00759-08;
RA   Agger S.A., Lopez-Gallego F., Hoye T.R., Schmidt-Dannert C.;
RT   "Identification of sesquiterpene synthases from Nostoc punctiforme PCC
RT   73102 and Nostoc sp. strain PCC 7120.";
RL   J. Bacteriol. 190:6084-6096(2008).
CC   -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate (FPP) to
CC       the sesquiterpene germacrene A. {ECO:0000269|PubMed:18658271}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = 5-epi-alpha-selinene +
CC         diphosphate; Xref=Rhea:RHEA:31819, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:63445, ChEBI:CHEBI:175763; EC=4.2.3.90;
CC         Evidence={ECO:0000269|PubMed:18658271};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.4 uM for FPP (at pH 8) {ECO:0000269|PubMed:18658271};
CC         Note=kcat is 0.044 sec(-1) with FPP as substrate (at pH 8).;
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   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; CP001037; ACC82216.1; -; Genomic_DNA.
DR   RefSeq; WP_012410187.1; NC_010628.1.
DR   AlphaFoldDB; B2J4A4; -.
DR   SMR; B2J4A4; -.
DR   STRING; 63737.Npun_R3832; -.
DR   EnsemblBacteria; ACC82216; ACC82216; Npun_R3832.
DR   KEGG; npu:Npun_R3832; -.
DR   eggNOG; COG0664; Bacteria.
DR   HOGENOM; CLU_042538_4_2_3; -.
DR   OMA; DLIEYAM; -.
DR   OrthoDB; 1869158at2; -.
DR   PhylomeDB; B2J4A4; -.
DR   Proteomes; UP000001191; Chromosome.
DR   GO; GO:0034005; F:germacrene-A synthase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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; Reference proteome.
FT   CHAIN           1..323
FT                   /note="Germacrene A synthase"
FT                   /id="PRO_0000418841"
FT   MOTIF           82..86
FT                   /note="DDXXD motif"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  38123 MW;  910D85B8B7B53777 CRC64;
     MNQLLCPGLY CPFPSQTNKY VDVLEEYSLE WVLRFNLLAN ESAYKRFCKS KFFFLAASAY
     PDSKFEELKI THDWLSWVFI WDDQCDLSEL KKQPEVLNNF HQRYLEILNG AELTSQDTLF
     SHALIDLRKR TLQRASIKWF NYFISYLEDY FYGCVQEATN RAKGIVPDLD TYIMIRRSSV
     GVYAVLALSE FCNQFIIPDV LRNHHLVKKL ELITTDIIAW SNDIFSASRE IASGDVHNLI
     FVLHYHKKIS LEKAIEQVVK IHNEEVHSLI KVESSLSFFS EELDVEITKY ISGMHSWIRG
     NLDWCYESYR YHNLERLELT EFK