GGPPS_MYCTU
ID GGPPS_MYCTU Reviewed; 350 AA.
AC O50410; I6X753; L0TCL7;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Geranylgeranyl diphosphate synthase {ECO:0000303|PubMed:23091471};
DE Short=GGPP synthase {ECO:0000303|PubMed:23091471};
DE Short=GGPS {ECO:0000305};
DE EC=2.5.1.29 {ECO:0000269|PubMed:23091471};
GN Name=idsB {ECO:0000312|EMBL:CCP46204.1};
GN OrderedLocusNames=Rv3383c {ECO:0000312|EMBL:CCP46204.1};
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=23091471; DOI=10.3389/fmicb.2012.00368;
RA Mann F.M., Xu M., Davenport E.K., Peters R.J.;
RT "Functional characterization and evolution of the isotuberculosinol operon
RT in Mycobacterium tuberculosis and related Mycobacteria.";
RL Front. Microbiol. 3:368-368(2012).
CC -!- FUNCTION: Catalyzes the condensation of isopentenyl pyrophosphate (IPP)
CC with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield geranylgeranyl
CC diphosphate (GGPP). {ECO:0000269|PubMed:23091471}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:23091471};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:23091471};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for IPP {ECO:0000269|PubMed:23091471};
CC KM=19 uM for FPP {ECO:0000269|PubMed:23091471};
CC Note=kcat is 1.0 min(-1). {ECO:0000269|PubMed:23091471};
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:23091471}.
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; CCP46204.1; -; Genomic_DNA.
DR RefSeq; NP_217900.1; NC_000962.3.
DR RefSeq; WP_009935184.1; NZ_NVQJ01000021.1.
DR AlphaFoldDB; O50410; -.
DR SMR; O50410; -.
DR STRING; 83332.Rv3383c; -.
DR PaxDb; O50410; -.
DR DNASU; 887680; -.
DR GeneID; 887680; -.
DR KEGG; mtu:Rv3383c; -.
DR PATRIC; fig|83332.111.peg.3771; -.
DR TubercuList; Rv3383c; -.
DR eggNOG; COG0142; Bacteria.
DR OMA; FPERLCE; -.
DR PhylomeDB; O50410; -.
DR UniPathway; UPA00389; UER00564.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0004311; F:farnesyltranstransferase 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:0033386; P:geranylgeranyl 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.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..350
FT /note="Geranylgeranyl diphosphate synthase"
FT /id="PRO_0000451296"
FT MOTIF 109..113
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT MOTIF 240..244
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 70
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 73
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 102
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 119
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 350 AA; 36432 MW; D777E023967F3B3C CRC64;
MGGVLTLDAA FLGSVPADLG KALLERARAD CGPVLHRAIE SMREPLATMA GYHLGWWNAD
RSTAAGSSGK YFRAALVYAA AAACGGDVGD ATPVSAAVEL VHNFTLLHDD VMDGDATRRG
RPTVWSVWGV GVAILLGDAL HATAVRILTG LTDECVAVRA IRRLQMSCLD LCIGQFEDCL
LEGQPEVTVD DYLRMAAGKT AALTGCCCAL GALVANADDA TIAALERFGH ELGLAFQCVD
DLIGIWGDPG VTGKPVGNDL ARRKATLPVV AALNSRSEAA TELAALYQAP AAMTASDVER
ATALVKVAGG GHVAQRCADE RIQAAIAALP DAVRSPDLIA LSQLICRREC
