ID A0A1U7ITX5_9CYAN Unreviewed; 405 AA.
AC A0A1U7ITX5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ferredoxin) {ECO:0000256|HAMAP-Rule:MF_00159};
DE EC=1.17.7.1 {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=NIES2119_01085 {ECO:0000313|EMBL:OKH40934.1};
OS [Phormidium ambiguum] IAM M-71.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Aerosakkonematales; Aerosakkonemataceae; Floridanema.
OX NCBI_TaxID=454136 {ECO:0000313|EMBL:OKH40934.1, ECO:0000313|Proteomes:UP000185860};
RN [1] {ECO:0000313|EMBL:OKH40934.1, ECO:0000313|Proteomes:UP000185860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM M-71 {ECO:0000313|EMBL:OKH40934.1,
RC ECO:0000313|Proteomes:UP000185860};
RA Zhu T., Hou S., Lu X., Hess W.R.;
RT "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT Habitats.";
RL Submitted (NOV-2016) 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 + 2 oxidized
CC [2Fe-2S]-[ferredoxin] + H2O = 2-C-methyl-D-erythritol 2,4-cyclic
CC diphosphate + 2 reduced [2Fe-2S]-[ferredoxin] + H(+);
CC Xref=Rhea:RHEA:26119, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:58483, ChEBI:CHEBI:128753;
CC EC=1.17.7.1; Evidence={ECO:0000256|ARBA:ARBA00051119,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKH40934.1}.
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DR EMBL; MRCE01000001; OKH40934.1; -; Genomic_DNA.
DR RefSeq; WP_073591608.1; NZ_MRCE01000001.1.
DR AlphaFoldDB; A0A1U7ITX5; -.
DR STRING; 454136.NIES2119_01085; -.
DR OrthoDB; 9803214at2; -.
DR UniPathway; UPA00056; UER00096.
DR Proteomes; UP000185860; Unassembled WGS sequence.
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: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:000005; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin); 1.
DR FunFam; 3.30.413.10:FF:000006; 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; 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}.
FT DOMAIN 25..296
FT /note="IspG TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF04551"
FT DOMAIN 310..397
FT /note="IspG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF26540"
FT BINDING 314
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 317
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 355
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
SQ SEQUENCE 405 AA; 44712 MW; 7DFC6447CF0419CF CRC64;
MQTLPNPATS TSQPEFETVI KRRKTRPVKV ANVTIGGGYP VVVQSMINED TMDIDGSVAA
IRRLHEIGCE IVRVTVPSVG HAKAVGEIKQ KLRETYQDVP LVADVHHNGM KIALEVAKYV
DKVRINPGLY VFEKPKPDRT EFTQAEIDEI GEKIRETLEP LVVSLRDQGK AMRIGVNHGS
LAERMLFTYG DTPEGMVESA IEFIRICESL DFRNLVISMK ASRVPVMVAA YRLMAKRMDE
LGMDYPLHLG VTEAGDGEYG RIKSTAGIAT LLADGIGDTI RVSLTEAPEK EIPVCYSILQ
ALGLRKTMVE YVACPSCGRT LFNLEEVLHK VREATKHLTG LDIAVMGCIV NGPGEMADAD
YGYVGKQPGF ISLYRGREEI KKVPESQGVE ELINLIKSDG RWVEP
//
