GFPPS_MYCTU
ID GFPPS_MYCTU Reviewed; 352 AA.
AC O53507; F2GJZ9; I6X3H6; Q7D7F1;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000305};
DE Short=E,E-FPP synthase {ECO:0000305};
DE Short=FPP synthase {ECO:0000305};
DE EC=2.5.1.10 {ECO:0000269|PubMed:32495977};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000305};
DE EC=2.5.1.1 {ECO:0000269|PubMed:32495977};
DE AltName: Full=Geranyl diphosphate synthase {ECO:0000305};
DE Short=GPP synthase {ECO:0000305};
GN Name=idsA2 {ECO:0000312|EMBL:CCP44950.1};
GN OrderedLocusNames=Rv2173 {ECO:0000312|EMBL:CCP44950.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX PubMed=32495977; DOI=10.1002/cbic.202000235;
RA Abe T., Ozaki S., Ueda D., Sato T.;
RT "Insight into isoprenoid biosynthesis by functional analysis of isoprenyl
RT diphosphate synthases from Mycobacterium vanbaalenii and Mycobacterium
RT tuberculosis.";
RL ChemBioChem 21:2931-2938(2020).
CC -!- FUNCTION: Catalyzes the sequential condensations of isopentenyl
CC pyrophosphate (IPP) with dimethylallyl diphosphate (DMAPP) to yield
CC geranyl diphosphate (GPP) and with GPP to yield (2E,6E)-farnesyl
CC diphosphate (E,E-FPP). {ECO:0000269|PubMed:32495977}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC Evidence={ECO:0000269|PubMed:32495977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22409;
CC Evidence={ECO:0000269|PubMed:32495977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC Evidence={ECO:0000269|PubMed:32495977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362;
CC Evidence={ECO:0000269|PubMed:32495977};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:32495977};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1. {ECO:0000269|PubMed:32495977}.
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate. {ECO:0000269|PubMed:32495977}.
CC -!- DOMAIN: Contains two aspartate-rich DDxxD motifs, designated as FARM
CC (the first aspartate-rich motif) and SARM (the second aspartate-rich
CC motif). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44950.1; -; Genomic_DNA.
DR RefSeq; NP_216689.1; NC_000962.3.
DR RefSeq; WP_003411245.1; NZ_NVQJ01000083.1.
DR AlphaFoldDB; O53507; -.
DR SMR; O53507; -.
DR STRING; 83332.Rv2173; -.
DR PaxDb; O53507; -.
DR PRIDE; O53507; -.
DR DNASU; 888334; -.
DR GeneID; 888334; -.
DR KEGG; mtu:Rv2173; -.
DR PATRIC; fig|83332.111.peg.2419; -.
DR TubercuList; Rv2173; -.
DR eggNOG; COG0142; Bacteria.
DR OMA; LELFQNW; -.
DR PhylomeDB; O53507; -.
DR UniPathway; UPA00259; UER00368.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..352
FT /note="(2E,6E)-farnesyl diphosphate synthase"
FT /id="PRO_0000451295"
FT MOTIF 84..88
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT MOTIF 236..240
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 43
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 46
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 77
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 94
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 352 AA; 37781 MW; 1DFC182CA1E529BF CRC64;
MAGAITDQLR RYLHGRRRAA AHMGSDYDGL IADLEDFVLG GGKRLRPLFA YWGWHAVASR
EPDPDVLLLF SALELLHAWA LVHDDLIDRS ATRRGRPTAQ LRYAALHRDR DWRGSPDQFG
MSAAILLGDL AQVWADDIVS KVCQSALAPD AQRRVHRVWA DIRNEVLGGQ YLDIVAEASA
AESIESAMNV ATLKTACYTV SRPLQLGTAA AADRSDVAAI FEHFGADLGV AFQLRDDVLG
VFGDPAVTGK PSGDDLKSGK RTVLVAEAVE LADRSDPLAA KLLRTSIGTR LTDAQVRELR
TVIEAVGARA AAESRIAALT QRALATLASA PINATAKAGL SELAMMAANR SA
