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ISPG_GLOVI
ID   ISPG_GLOVI              Reviewed;         396 AA.
AC   Q7NFA4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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};
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=gll3622;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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 + 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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00159};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00159}.
CC   -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00159}.
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DR   EMBL; BA000045; BAC91563.1; -; Genomic_DNA.
DR   RefSeq; NP_926568.1; NC_005125.1.
DR   RefSeq; WP_011143611.1; NC_005125.1.
DR   AlphaFoldDB; Q7NFA4; -.
DR   SMR; Q7NFA4; -.
DR   STRING; 251221.35214194; -.
DR   EnsemblBacteria; BAC91563; BAC91563; BAC91563.
DR   KEGG; gvi:gll3622; -.
DR   PATRIC; fig|251221.4.peg.3656; -.
DR   eggNOG; COG0821; Bacteria.
DR   HOGENOM; CLU_042258_0_0_3; -.
DR   InParanoid; Q7NFA4; -.
DR   OMA; PTCGRTQ; -.
DR   OrthoDB; 665306at2; -.
DR   PhylomeDB; Q7NFA4; -.
DR   UniPathway; UPA00056; UER00096.
DR   Proteomes; UP000000557; 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; 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   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..396
FT                   /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT                   (ferredoxin)"
FT                   /id="PRO_0000190582"
FT   BINDING         305
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         308
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         339
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         346
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ   SEQUENCE   396 AA;  43158 MW;  5894380901510027 CRC64;
     MQTLDPVTPA LLPLRRVTRP VQVGALTIGG NAPVVVQSMI NEDTLDTPGA VAAIRALHKA
     GCELVRVTVP SLAHARALER IRKTLEDTYR PVPLVADVHH DGGPIALEVA RHVDKVRINP
     GLFVFRRARL GDYTAEDVER ARAQIREELK PLVDVLGAQD KAMRIGVNHG SLSERMLYIH
     GDTPEGMVQS AVEFVEICEQ LGYHNLVISL KASRVPVMIA VYRLAAKLLD ARGMHYPFHL
     GVTEAGDGEY GRIKSTAGIA TLLADGIGDT IRVSLTEDPL KEIPVCYGIL QALGLRRTMV
     EYVACPSCGR TLFNLETVLH RVREATRHLT GLNIAVMGCI VNGPGEMADA DYGYVGKTPG
     TISLYRGREE IKKVPEARGV EALVDLIKSD GRWVDP
 
 
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