ID A0A0P9CPX2_9BACL Unreviewed; 322 AA.
AC A0A0P9CPX2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Heptaprenyl diphosphate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AN477_05230 {ECO:0000313|EMBL:KPV44882.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV44882.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV44882.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV44882.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00006706, ECO:0000256|RuleBase:RU004466}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV44882.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJCO01000020; KPV44882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9CPX2; -.
DR STRING; 471514.AN477_05230; -.
DR PATRIC; fig|471514.4.peg.3216; -.
DR Proteomes; UP000050482; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; 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; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR12001:SF87; OCTAPRENYL DIPHOSPHATE SYNTHASE; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000050482};
KW Transferase {ECO:0000256|RuleBase:RU004466};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 322 AA; 35576 MW; 5D988A2428597214 CRC64;
MDFRQVYEQY QHDLQEIDNI LGTSMESENA LLAGSSRQLL AAGGKRIRPL FALLCSELGK
MSEKQSVHRL AASVELVHMA SLVHDDVIDD ATVRRGHPTV RAQYGNRPAM YTGDFLFARA
IRLLSSLSNM SLHVEMSNAI VRMTEGEIDQ IRDFYDLGQP LKKYLRRIER KTALLISVSC
SLGAVVGGAP AAAVKAARRF GYFTGMAFQV IDDILDFSGT ESLVGKPVGN DLWQGNITYP
ALYTAQCTAQ GAQLRNLVSP TMTRDDLNAA VALVRESGAL EQANQLASRY LDKALVILRG
LDESSTRRSL EVVARFVNQR MF
//