ID   F2K4H8_MARM1            Unreviewed;       301 AA.
AC   F2K4H8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Geranyltranstransferase {ECO:0000313|EMBL:ADZ90277.1};
DE            EC=2.5.1.10 {ECO:0000313|EMBL:ADZ90277.1};
GN   OrderedLocusNames=Marme_1002 {ECO:0000313|EMBL:ADZ90277.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS   MMB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90277.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|EMBL:ADZ90277.1, ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RX   PubMed=22675599; DOI=10.4056/sigs.2545743;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA   Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT   mediterranea type strain (MMB-1(T)).";
RL   Stand. Genomic Sci. 6:63-73(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC       {ECO:0000256|RuleBase:RU004466}.
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DR   EMBL; CP002583; ADZ90277.1; -; Genomic_DNA.
DR   RefSeq; WP_013660182.1; NZ_CP047696.1.
DR   AlphaFoldDB; F2K4H8; -.
DR   STRING; 717774.Marme_1002; -.
DR   KEGG; mme:Marme_1002; -.
DR   PATRIC; fig|717774.3.peg.1044; -.
DR   eggNOG; COG0142; Bacteria.
DR   HOGENOM; CLU_014015_0_1_6; -.
DR   OrthoDB; 9805316at2; -.
DR   Proteomes; UP000001062; Chromosome.
DR   GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   PANTHER; PTHR43281; FARNESYL DIPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR43281:SF1; FARNESYL DIPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001062};
KW   Transferase {ECO:0000256|RuleBase:RU004466, ECO:0000313|EMBL:ADZ90277.1}.
SQ   SEQUENCE   301 AA;  33573 MW;  AB8C1B7034849610 CRC64;
     MNLEQFSHYS RDRVDRYLND QLTQYDAADY LHEAMRYSLF NGGKRVRPML VYATAELFSE
     SNRLTDASAA AIESIHAYSL IHDDLPAMDD DDLRRGKPTC HIQFDEATAI LTGDALQTFA
     FELLSASYNE IDTDNLADCK TRQLRLIRSL SRASGRFGMV TGQMIDLNNV DRSITLETLE
     KMHQHKTGAL IRASVLMGAQ SVGIEDQKIL SQLDKYASAI GLAFQVQDDI IDITSDTQTL
     GKNQFSDSEA NKPTYPKLLG LEGAREKANT LKQEAIEAIS PFGDKAAPLI QLASYIISRN
     H
//