ISPG_ECO27
ID ISPG_ECO27 Reviewed; 372 AA.
AC B7UGW1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000255|HAMAP-Rule:MF_00159};
DE EC=1.17.7.3 {ECO:0000255|HAMAP-Rule:MF_00159};
DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00159};
GN Name=ispG {ECO:0000255|HAMAP-Rule:MF_00159}; OrderedLocusNames=E2348C_2798;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-
CC 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O +
CC oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic
CC diphosphate + reduced [flavodoxin]; Xref=Rhea:RHEA:43604, Rhea:RHEA-
CC COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:58483, ChEBI:CHEBI:128753; EC=1.17.7.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00159};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00159};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00159};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 5/6. {ECO:0000255|HAMAP-Rule:MF_00159}.
CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP-
CC Rule:MF_00159}.
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DR EMBL; FM180568; CAS10346.1; -; Genomic_DNA.
DR RefSeq; WP_000551807.1; NC_011601.1.
DR AlphaFoldDB; B7UGW1; -.
DR SMR; B7UGW1; -.
DR EnsemblBacteria; CAS10346; CAS10346; E2348C_2798.
DR GeneID; 60903826; -.
DR GeneID; 67416899; -.
DR KEGG; ecg:E2348C_2798; -.
DR HOGENOM; CLU_042258_0_0_6; -.
DR OMA; PTCGRTQ; -.
DR UniPathway; UPA00056; UER00096.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.30.413.10; -; 1.
DR HAMAP; MF_00159; IspG; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR016425; IspG_bac.
DR InterPro; IPR004588; IspG_bac-typ.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR PANTHER; PTHR30454; PTHR30454; 1.
DR Pfam; PF04551; GcpE; 1.
DR PIRSF; PIRSF004640; IspG; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR00612; ispG_gcpE; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW Oxidoreductase.
FT CHAIN 1..372
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (flavodoxin)"
FT /id="PRO_1000123444"
FT BINDING 270
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 273
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 305
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ SEQUENCE 372 AA; 40684 MW; 3666FD83D5CD4F9F CRC64;
MHNQAPIQRR KSTRIYVGNV PIGDGAPIAV QSMTNTRTTD VEATVNQIKA LERVGADIVR
VSVPTMDAAE AFKLIKQQVN VPLVADIHFD YRIALKVAEY GVDCLRINPG NIGNEERIRM
VVDCARDKNI PIRIGVNAGS LEKDLQEKYG EPTPQALLES AMRHVDHLDR LNFDQFKVSV
KASDVFLAVE SYRLLAKQID QPLHLGITEA GGARSGAVKS AIGLGLLLSE GIGDTLRVSL
AADPVEEIKV GFDILKSLRI RSRGINFIAC PTCSRQEFDV IGTVNALEQR LEDIITPMDV
SIIGCVVNGP GEALVSTLGV TGGNKKSGLY EDGVRKDRLD NNDMIDQLEA RIRAKASQLD
EARRIDVQQV EK
