ID Q4K5A6_PSEF5 Unreviewed; 295 AA.
AC Q4K5A6;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Geranyltranstransferase {ECO:0000313|EMBL:AAY94715.1};
DE EC=2.5.1.10 {ECO:0000313|EMBL:AAY94715.1};
GN Name=ispA {ECO:0000313|EMBL:AAY94715.1};
GN OrderedLocusNames=PFL_5509 {ECO:0000313|EMBL:AAY94715.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY94715.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY94715.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
RN [2] {ECO:0007829|PDB:3LJI}
RP X-RAY CRYSTALLOGRAPHY (1.39 ANGSTROMS) OF 3-295.
RA Malashkevich V.N., Toro R., Patskovsky Y., Sauder J.M., Burley S.K.,
RA Almo S.C.;
RT "CRYSTAL STRUCTURE OF putative geranyltranstransferase from Pseudomonas
RT fluorescens Pf-5.";
RL Submitted (JAN-2010) to the PDB data bank.
RN [3] {ECO:0007829|PDB:3LSN}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 3-295 IN COMPLEX WITH MAGNESIUM.
RA Malashkevich V.N., Toro R., Sauder J.M., Burley S.K., Almo S.C.;
RT "Crystal structure of putative geranyltranstransferase from Pseudomonas
RT fluorescens PF-5 complexed with magnesium.";
RL Submitted (FEB-2010) to the PDB data bank.
RN [4] {ECO:0007829|PDB:3P41}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 3-295 IN COMPLEX WITH MG(2+).
RX PubMed=23493556; DOI=10.1073/pnas.1300632110;
RA Wallrapp F.H., Pan J.J., Ramamoorthy G., Almonacid D.E., Hillerich B.S.,
RA Seidel R., Patskovsky Y., Babbitt P.C., Almo S.C., Jacobson M.P.,
RA Poulter C.D.;
RT "Prediction of function for the polyprenyl transferase subgroup in the
RT isoprenoid synthase superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1196-E1202(2013).
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; CP000076; AAY94715.1; -; Genomic_DNA.
DR RefSeq; WP_011063725.1; NC_004129.6.
DR PDB; 3LJI; X-ray; 1.39 A; A=3-295.
DR PDB; 3LSN; X-ray; 1.35 A; A=3-295.
DR PDB; 3P41; X-ray; 1.76 A; A=3-295.
DR PDBsum; 3LJI; -.
DR PDBsum; 3LSN; -.
DR PDBsum; 3P41; -.
DR AlphaFoldDB; Q4K5A6; -.
DR SMR; Q4K5A6; -.
DR STRING; 220664.PFL_5509; -.
DR DNASU; 3479897; -.
DR KEGG; pfl:PFL_5509; -.
DR PATRIC; fig|220664.5.peg.5624; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_0_1_6; -.
DR EvolutionaryTrace; Q4K5A6; -.
DR Proteomes; UP000008540; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3LJI, ECO:0007829|PDB:3LSN};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0007829|PDB:3LSN, ECO:0007829|PDB:3P41};
KW Transferase {ECO:0000256|RuleBase:RU004466, ECO:0000313|EMBL:AAY94715.1}.
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:3P41"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LSN"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:3P41"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LSN"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:3LSN"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:3LSN"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0007829|PDB:3LSN, ECO:0007829|PDB:3P41"
SQ SEQUENCE 295 AA; 31397 MW; 4FB774360749E9A0 CRC64;
MITAYQASSQ ARVDAAMHTL FTAPSPELAR LYEAMRYSVM NGGKRVRPLL AYAACEALGG
KPEQANGAAC AVELIHAYSL VHDDLPAMDD DDLRRGQPTT HKAFDEACAI LAGDGLQSLA
FSALLDPALS DASAEIRLRM VTTLAQAAGP AGMVGGQAID LGSVGLKLDQ QALEYMHRHK
TGALIEASVI LGALASGRAE KGELKALQTY AQAIGLAFQV QDDILDVESD TATLGKRQGA
DIARDKPTYP ALLGLAAAKE YALELRDQAL HALRPFDAAA EPLRELARYI VERRS
//
