ISPG_THET2
ID ISPG_THET2 Reviewed; 406 AA.
AC Q72H18;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=TT_C1677;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S), COFACTOR, AND SUBUNIT.
RX PubMed=21167158; DOI=10.1016/j.febslet.2010.12.012;
RA Rekittke I., Nonaka T., Wiesner J., Demmer U., Warkentin E., Jomaa H.,
RA Ermler U.;
RT "Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate synthase
RT (GcpE) from Thermus thermophilus.";
RL FEBS Lett. 585:447-451(2011).
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 ECO:0000269|PubMed:21167158};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00159, ECO:0000269|PubMed:21167158};
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:21167158}.
CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP-
CC Rule:MF_00159}.
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DR EMBL; AE017221; AAS82019.1; -; Genomic_DNA.
DR RefSeq; WP_011174043.1; NC_005835.1.
DR PDB; 2Y0F; X-ray; 2.50 A; A/B/C/D=1-406.
DR PDB; 4G9P; X-ray; 1.55 A; A=1-406.
DR PDBsum; 2Y0F; -.
DR PDBsum; 4G9P; -.
DR AlphaFoldDB; Q72H18; -.
DR SMR; Q72H18; -.
DR STRING; 262724.TT_C1677; -.
DR EnsemblBacteria; AAS82019; AAS82019; TT_C1677.
DR KEGG; tth:TT_C1677; -.
DR eggNOG; COG0821; Bacteria.
DR HOGENOM; CLU_042258_1_0_0; -.
DR OMA; PTCGRTQ; -.
DR OrthoDB; 665306at2; -.
DR BRENDA; 1.17.7.3; 2305.
DR UniPathway; UPA00056; UER00096.
DR EvolutionaryTrace; Q72H18; -.
DR Proteomes; UP000000592; 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; 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; SSF51717; SSF51717; 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.
FT CHAIN 1..406
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (flavodoxin)"
FT /id="PRO_0000190644"
FT BINDING 297
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159,
FT ECO:0000269|PubMed:21167158"
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:21167158"
FT BINDING 343
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159,
FT ECO:0000269|PubMed:21167158"
FT BINDING 350
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159,
FT ECO:0000269|PubMed:21167158"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 170..192
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 236..252
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:2Y0F"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 305..329
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:4G9P"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:4G9P"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:4G9P"
FT HELIX 386..401
FT /evidence="ECO:0007829|PDB:4G9P"
SQ SEQUENCE 406 AA; 44217 MW; F6DA1B69F28093B0 CRC64;
MEGMRRPTPT VYVGRVPIGG AHPIAVQSMT NTPTRDVEAT TAQVLELHRA GSEIVRLTVN
DEEAAKAVPE IKRRLLAEGV EVPLVGDFHF NGHLLLRKYP KMAEALDKFR INPGTLGRGR
HKDEHFAEMI RIAMDLGKPV RIGANWGSLD PALLTELMDR NASRPEPKSA HEVVLEALVE
SAVRAYEAAL EMGLGEDKLV LSAKVSKARD LVWVYRELAR RTQAPLHLGL TEAGMGVKGI
VASAAALAPL LLEGIGDTIR VSLTPSPKEP RTKEVEVAQE ILQALGLRAF APEVTSCPGC
GRTTSTFFQE LAEEVSRRLK ERLPEWRARY PGVEELKVAV MGCVVNGPGE SKHAHIGISL
PGAGEEPKAP VYADGKLLTI LKGEGIAEEF LRLVEDYVKT RFAPKA
