ZFPP_MYCS2
ID ZFPP_MYCS2 Reviewed; 263 AA.
AC A0R2W4; I7G761;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=(2Z,6E)-farnesyl diphosphate synthase;
DE EC=2.5.1.68 {ECO:0000269|PubMed:11004176};
DE AltName: Full=Short-chain Z-isoprenyl diphosphate synthase;
DE AltName: Full=Z-FPP synthase;
DE Short=Z-FPPS;
DE AltName: Full=Z-Polyprenyl diphosphate synthase;
DE AltName: Full=Z-isoprenyl diphosphate synthase;
GN Name=uppS; OrderedLocusNames=MSMEG_5256, MSMEI_5118;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=4741910; DOI=10.1016/0005-2760(73)90011-8;
RA Takayama K., Schnoes H.K., Semmler E.J.;
RT "Characterization of the alkali-stable mannophospholipids of Mycobacterium
RT smegmatis.";
RL Biochim. Biophys. Acta 316:212-221(1973).
RN [5]
RP FUNCTION AS A FARNESYL DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11004176; DOI=10.1128/jb.182.20.5771-5778.2000;
RA Crick D.C., Schulbach M.C., Zink E.E., Macchia M., Barontini S.,
RA Besra G.S., Brennan P.J.;
RT "Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and
RT Mycobacterium smegmatis.";
RL J. Bacteriol. 182:5771-5778(2000).
CC -!- FUNCTION: Catalyzes the condensation of only one isopentenyl
CC pyrophosphate (IPP) unit in the cis configuration to E-geranyl
CC diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl
CC diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl
CC diphosphate, which has a central role in the biosynthesis of the
CC mycobacterial cell wall. {ECO:0000269|PubMed:11004176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:162247; EC=2.5.1.68;
CC Evidence={ECO:0000269|PubMed:11004176};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WFF5};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:P9WFF5};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WFF5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11004176,
CC ECO:0000269|PubMed:4741910}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. Z-FPP synthase
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000480; ABK70340.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41562.1; -; Genomic_DNA.
DR RefSeq; WP_003896657.1; NZ_SIJM01000014.1.
DR RefSeq; YP_889502.1; NC_008596.1.
DR AlphaFoldDB; A0R2W4; -.
DR SMR; A0R2W4; -.
DR STRING; 246196.MSMEI_5118; -.
DR PRIDE; A0R2W4; -.
DR EnsemblBacteria; ABK70340; ABK70340; MSMEG_5256.
DR EnsemblBacteria; AFP41562; AFP41562; MSMEI_5118.
DR GeneID; 66736570; -.
DR KEGG; msg:MSMEI_5118; -.
DR KEGG; msm:MSMEG_5256; -.
DR PATRIC; fig|246196.19.peg.5127; -.
DR eggNOG; COG0020; Bacteria.
DR OMA; TKGQPDP; -.
DR OrthoDB; 1630604at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033850; F:Z-farnesyl diphosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0016094; P:polyprenol biosynthetic process; ISS:UniProtKB.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Magnesium; Membrane; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..263
FT /note="(2Z,6E)-farnesyl diphosphate synthase"
FT /id="PRO_0000417571"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 41..44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218..220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Important for determining product length"
FT /evidence="ECO:0000250"
SQ SEQUENCE 263 AA; 29935 MW; C22ABBD9F9A6EF1F CRC64;
MDIIPPRLKE PAYRIYEMRL RHELVRSKAQ LPRHIAVLCD GNRRWARDAG YDDVSIGYRK
GAAKIAEMLR WCQAAGIEMA TIYLLSTENL QRDPDELTAL IEIITDVVEE ICAPYNKWSV
RTVGDLELLG DEPARRLREA VESTTTKGAN FHVNVAVAYG GRQEIVDAVR SLLSKELANG
ATAEQLIEAV TVDGISENLY TSGQPDPDLV IRTSGEQRLS GFLLWQSAYS EMWFTEAYWP
AFRRVDFLRA LRDYTARHRR FGK
