ISPG_PSEP1
ID ISPG_PSEP1 Reviewed; 369 AA.
AC A5VYT5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Pput_0883;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000712; ABQ77045.1; -; Genomic_DNA.
DR RefSeq; WP_003248517.1; NC_009512.1.
DR AlphaFoldDB; A5VYT5; -.
DR SMR; A5VYT5; -.
DR STRING; 351746.Pput_0883; -.
DR PRIDE; A5VYT5; -.
DR EnsemblBacteria; ABQ77045; ABQ77045; Pput_0883.
DR KEGG; ppf:Pput_0883; -.
DR eggNOG; COG0821; Bacteria.
DR HOGENOM; CLU_042258_0_0_6; -.
DR OMA; PTCGRTQ; -.
DR OrthoDB; 665306at2; -.
DR UniPathway; UPA00056; UER00096.
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; 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..369
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (flavodoxin)"
FT /id="PRO_1000011502"
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 369 AA; 39716 MW; 94A550CC0FC795AB CRC64;
MHGESPIKRR ESRKIWVGNV PVGGDAPIAV QSMTNTDTND VAATVAQIQR LVDAGVDIVR
VSVPDMDAAE AFGKIKQRVS VPLVADIHFD YKIALRVAEL GVDCLRINPG NIGREDRVRA
VVDAARDRGI PIRIGVNAGS LEKDLQKKYG EPTPAALVES ALRHVEHLDR LDFQDFKVSV
KASDVFMAVE AYRLLAKQIV QPLHLGITEA GGLRSGTVKS AVGLGMLLAE GIGDTIRISL
AADPVEEVKV GYDILKSLHL RSRGINFIAC PSCSRQNFDV VKTMNELEGR LEDLLVPLDV
AVIGCVVNGP GEAKEAHVGL TGGTPNLIYI DGKPAQKLTN DNLVDELEKL IRQKAAEKAE
ADAALIVRG
