ISPG_THEVB
ID ISPG_THEVB Reviewed; 402 AA.
AC Q8DK70;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ferredoxin) {ECO:0000255|HAMAP-Rule:MF_00159};
DE EC=1.17.7.1 {ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:15792953};
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=tlr0996;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INTERACTION WITH PETF.
RX PubMed=15792953; DOI=10.1074/jbc.m500865200;
RA Okada K., Hase T.;
RT "Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl
RT diphosphate synthase interacts with ferredoxin in Thermosynechococcus
RT elongatus BP-1.";
RL J. Biol. Chem. 280:20672-20679(2005).
CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-
CC 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using
CC ferredoxin I (PetF) as the reducing agent. {ECO:0000255|HAMAP-
CC Rule:MF_00159, ECO:0000269|PubMed:15792953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + H2O + 2
CC oxidized [2Fe-2S]-[ferredoxin] = 2-C-methyl-D-erythritol 2,4-cyclic
CC diphosphate + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
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:0000255|HAMAP-Rule:MF_00159,
CC ECO:0000269|PubMed:15792953};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00159,
CC ECO:0000269|PubMed:15792953};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00159,
CC ECO:0000269|PubMed:15792953};
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 -!- INTERACTION:
CC Q8DK70; P0A3C9: petF1; NbExp=3; IntAct=EBI-766800, EBI-766786;
CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP-
CC Rule:MF_00159}.
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DR EMBL; BA000039; BAC08548.1; -; Genomic_DNA.
DR RefSeq; NP_681786.1; NC_004113.1.
DR RefSeq; WP_011056840.1; NC_004113.1.
DR AlphaFoldDB; Q8DK70; -.
DR SMR; Q8DK70; -.
DR IntAct; Q8DK70; 1.
DR STRING; 197221.22294719; -.
DR EnsemblBacteria; BAC08548; BAC08548; BAC08548.
DR KEGG; tel:tlr0996; -.
DR PATRIC; fig|197221.4.peg.1047; -.
DR eggNOG; COG0821; Bacteria.
DR OMA; PTCGRTQ; -.
DR OrthoDB; 665306at2; -.
DR BRENDA; 1.17.7.1; 7763.
DR UniPathway; UPA00056; UER00096.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..402
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (ferredoxin)"
FT /id="PRO_0000190638"
FT BINDING 311
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 314
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 345
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 352
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ SEQUENCE 402 AA; 44192 MW; 7595FFC940AC60D7 CRC64;
MQTLPSPVQA TPTETAIVRR KTRPVPIGSV VIGGGHPVAV QSMINEDTLD IEGSVAAIRR
LHEIGCEIVR VTVPSLAHAK AMEEIRDRLY KTYKPVPLVA DVHHNGMKIA LEVAKYVDNV
RINPGLYVFE KPKPNRTEYT QAEFDEIGAK IRETLEPLVI SLRDQGKSMR IGVNHGSLAE
RMLFTYGDTP EGMVESALEF IRICESLNFY NLEISLKASR VPVMIAANRL MVKRMDELGM
DYPLHLGVTE AGDGEYGRIK STAGIATLLA EGIGDTIRVS LTEAPEKEIP VCYGILQALG
LRRTMVEYVA CPSCGRTLFN LEEVLHKVRE ATKHLTGLNI AVMGCIVNGP GEMADADYGY
VGKQPGYISL YRGREEVKKV PEAEGVAALV ELIKADGRWV DP
