ID A0A1V0HKD7_9ENTR Unreviewed; 376 AA.
AC A0A1V0HKD7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000256|HAMAP-Rule:MF_00159};
DE EC=1.17.7.3 {ECO:0000256|HAMAP-Rule:MF_00159};
DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00159};
GN Name=ispG {ECO:0000256|HAMAP-Rule:MF_00159};
GN ORFNames=AOQ87_01170 {ECO:0000313|EMBL:ARC53290.1};
OS Candidatus Riesia pediculischaeffi.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Enterobacteriaceae; Candidatus Riesia.
OX NCBI_TaxID=428411 {ECO:0000313|EMBL:ARC53290.1, ECO:0000313|Proteomes:UP000242793};
RN [1] {ECO:0000313|EMBL:ARC53290.1, ECO:0000313|Proteomes:UP000242793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSK {ECO:0000313|EMBL:ARC53290.1,
RC ECO:0000313|Proteomes:UP000242793};
RA Boyd B.M.;
RT "Survey of human and primate louse endosymbionts.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate
CC (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
CC {ECO:0000256|HAMAP-Rule:MF_00159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + oxidized
CC [flavodoxin] + H2O + 2 H(+) = 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:0000256|HAMAP-Rule:MF_00159};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00159};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00159}.
CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000256|HAMAP-
CC Rule:MF_00159}.
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DR EMBL; CP012839; ARC53290.1; -; Genomic_DNA.
DR RefSeq; WP_080626528.1; NZ_CP012839.1.
DR AlphaFoldDB; A0A1V0HKD7; -.
DR STRING; 428411.AOQ87_01170; -.
DR KEGG; rped:AOQ87_01170; -.
DR UniPathway; UPA00056; UER00096.
DR Proteomes; UP000242793; 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 (ferredoxin); IEA:UniProtKB-UniRule.
DR GO; GO:0141197; F:4-hydroxy-3-methylbut-2-enyl-diphosphate synthase activity (flavodoxin); IEA:UniProtKB-EC.
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-UniRule.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR FunFam; 3.20.20.20:FF:000001; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin); 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR HAMAP; MF_00159; IspG; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR016425; IspG_bac.
DR InterPro; IPR004588; IspG_bac-typ.
DR InterPro; IPR058579; IspG_C.
DR InterPro; IPR058578; IspG_TIM.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR NCBIfam; TIGR00612; ispG_gcpE; 1.
DR NCBIfam; NF001540; PRK00366.1; 1.
DR PANTHER; PTHR30454; 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR30454:SF0; 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE (FERREDOXIN), CHLOROPLASTIC; 1.
DR Pfam; PF04551; GcpE; 1.
DR Pfam; PF26540; GcpE_C; 1.
DR PIRSF; PIRSF004640; IspG; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00159};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00159};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00159};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00159};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00159};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00159}; Reference proteome {ECO:0000313|Proteomes:UP000242793}.
FT DOMAIN 12..251
FT /note="IspG TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF04551"
FT DOMAIN 266..354
FT /note="IspG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF26540"
FT BINDING 270
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 273
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 305
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
SQ SEQUENCE 376 AA; 41434 MW; 99CF29AB569E0BB9 CRC64;
MKKQSIVKRR KTKKIYVGNV PIGQGSRISV QSMTNTSTLD VSETVKQVRS LNDAGADIVR
ISVPTMDSAE AFKKIKKQVD VPIVADVHFN YRIALKVIQY GADCLRINPG NIGNYDKIRM
ITQSAKDENV SIRIGVNSGS LEEDIKRSYG GSTAEALVHS AVRQIDIFDK LNFDQFKVSV
KSSDVLTSIM AYRLLSSRTD QPIHLGITES GGRRNGSIRS AIGIGSLLLD GIGDTLRVSL
ADDPVEEVKV ALSILNSLKI RSVGVQIVAC PTCSRKEFDV INVVKVLEER LSDVKDPLKI
SVIGCVVNGF GEAENSDFGI IGRRTRSVLL NRVENKKKFV HNDIISEELE DEVRKVIEIR
ERKCGSNCQS NSKQES
//
