ISPG_AQUAE
ID ISPG_AQUAE Reviewed; 357 AA.
AC O67496;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
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}; Synonyms=gcpE;
GN OrderedLocusNames=aq_1540;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S), FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLN-26; ARG-55;
RP ASP-81; ARG-101; ASN-103; ASN-106; ARG-128; ASN-132; GLU-204; GLU-242;
RP ARG-256 AND GLU-307.
RX PubMed=20932974; DOI=10.1016/j.jmb.2010.09.050;
RA Lee M., Graewert T., Quitterer F., Rohdich F., Eppinger J., Eisenreich W.,
RA Bacher A., Groll M.;
RT "Biosynthesis of isoprenoids: crystal structure of the [4Fe-4S] cluster
RT protein IspG.";
RL J. Mol. Biol. 404:600-610(2010).
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, ECO:0000269|PubMed:20932974}.
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 ECO:0000269|PubMed:20932974};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00159, ECO:0000269|PubMed:20932974};
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20932974}.
CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP-
CC Rule:MF_00159}.
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DR EMBL; AE000657; AAC07467.1; -; Genomic_DNA.
DR PIR; F70433; F70433.
DR RefSeq; NP_214061.1; NC_000918.1.
DR RefSeq; WP_010880999.1; NC_000918.1.
DR PDB; 3NOY; X-ray; 2.70 A; A/B/C/D=1-357.
DR PDBsum; 3NOY; -.
DR AlphaFoldDB; O67496; -.
DR SMR; O67496; -.
DR STRING; 224324.aq_1540; -.
DR EnsemblBacteria; AAC07467; AAC07467; aq_1540.
DR KEGG; aae:aq_1540; -.
DR PATRIC; fig|224324.8.peg.1195; -.
DR eggNOG; COG0821; Bacteria.
DR HOGENOM; CLU_042258_0_0_0; -.
DR InParanoid; O67496; -.
DR OMA; PTCGRTQ; -.
DR OrthoDB; 665306at2; -.
DR UniPathway; UPA00056; UER00096.
DR EvolutionaryTrace; O67496; -.
DR Proteomes; UP000000798; 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; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central.
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; IPR036849; Enolase-like_C_sf.
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; SSF51604; SSF51604; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR00612; ispG_gcpE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..357
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (flavodoxin)"
FT /id="PRO_0000190525"
FT BINDING 265
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159,
FT ECO:0000269|PubMed:20932974"
FT BINDING 268
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159,
FT ECO:0000269|PubMed:20932974"
FT BINDING 300
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159,
FT ECO:0000269|PubMed:20932974"
FT BINDING 307
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159,
FT ECO:0000269|PubMed:20932974"
FT MUTAGEN 26
FT /note="Q->E: Reduces activity 100-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 55
FT /note="R->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 81
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 101
FT /note="R->K: Reduces activity 500-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 103
FT /note="N->D: Reduces activity 200-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 106
FT /note="N->D: Reduces activity 2-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 128
FT /note="R->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 132
FT /note="N->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 204
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 242
FT /note="E->Q: Reduces activity 12-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 256
FT /note="R->K: Reduces activity 2-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 307
FT /note="E->C: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 307
FT /note="E->D: Reduces activity 500-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT MUTAGEN 307
FT /note="E->Q: Reduces activity 4-fold."
FT /evidence="ECO:0000269|PubMed:20932974"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3NOY"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:3NOY"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:3NOY"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:3NOY"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:3NOY"
SQ SEQUENCE 357 AA; 39128 MW; 85680BCCFA7AF9D5 CRC64;
MIQKRKTRQI RVGNVKIGGD APIVVQSMTS TKTHDVEATL NQIKRLYEAG CEIVRVAVPH
KEDVEALEEI VKKSPMPVIA DIHFAPSYAF LSMEKGVHGI RINPGNIGKE EIVREIVEEA
KRRGVAVRIG VNSGSLEKDL LEKYGYPSAE ALAESALRWS EKFEKWGFTN YKVSIKGSDV
LQNVRANLIF AERTDVPLHI GITEAGMGTK GIIKSSVGIG ILLYMGIGDT VRVSLTDDPV
VEVETAYEIL KSLGLRRRGV EIVACPTCGR IEVDLPKVVK EVQEKLSGVK TPLKVAVMGC
VVNAIGEARE ADIGLACGRG FAWLFKHGKP IKKVDESEMV DELLKEIQNM EKDGGTN
