ID Q6A9S7_CUTAK Unreviewed; 365 AA.
AC Q6A9S7;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Geranylgeranyl pyrophosphate synthase {ECO:0000313|EMBL:AAT82489.1};
DE EC=2.5.1.1 {ECO:0000313|EMBL:AAT82489.1};
GN OrderedLocusNames=PPA0732 {ECO:0000313|EMBL:AAT82489.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT82489.1, ECO:0000313|Proteomes:UP000000603};
RN [1] {ECO:0000313|EMBL:AAT82489.1, ECO:0000313|Proteomes:UP000000603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC {ECO:0000256|ARBA:ARBA00006706, ECO:0000256|RuleBase:RU004466}.
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DR EMBL; AE017283; AAT82489.1; -; Genomic_DNA.
DR RefSeq; WP_002513952.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A9S7; -.
DR SMR; Q6A9S7; -.
DR EnsemblBacteria; AAT82489; AAT82489; PPA0732.
DR KEGG; pac:PPA0732; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_2_1_11; -.
DR Proteomes; UP000000603; Chromosome.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
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; PTHR12001:SF88; (2E,6E)-FARNESYL DIPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE 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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Transferase {ECO:0000256|RuleBase:RU004466, ECO:0000313|EMBL:AAT82489.1}.
SQ SEQUENCE 365 AA; 39220 MW; 925F2C9339C99C19 CRC64;
MYPFDPSSPV SADFRDSVSA RILSFLDDEK RVIDAIGAEL SPVLDAARDY TAGGKRLRPA
FCYWGHAAAA DQPTEPAGLL QAAASLEFLH VSALVHDDLM DHSDTRRGLP SVHRHFEAAH
GIAHGDGPAE QFGFDIAILL GDLLLMWSSQ MFTSAPVKAD RLAAATPLLD AMRTEVTCGQ
VLDVTSQSGM AGSDSESALD LVGRVVEYKC ASYTVVRPCQ IGVALAGGSD RLQQTMADFG
SPIGRAFQYR DDLLGVFGDA ELTGKPAGDD LREGKRTVLV AHALNRADSH DAARLKSLLG
RPDLDDNDVA TARRIIETSG AREAVESTIV QCHDHAIAVL DDAEMTDAGR IALRELARQC
VERHF
//
