ID   ISPG_MACCJ              Reviewed;         371 AA.
AC   B9E6U1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=MCCL_1202;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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       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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009484; BAH17909.1; -; Genomic_DNA.
DR   RefSeq; WP_012657107.1; NC_011999.1.
DR   AlphaFoldDB; B9E6U1; -.
DR   SMR; B9E6U1; -.
DR   STRING; 458233.MCCL_1202; -.
DR   EnsemblBacteria; BAH17909; BAH17909; MCCL_1202.
DR   KEGG; mcl:MCCL_1202; -.
DR   eggNOG; COG0821; Bacteria.
DR   HOGENOM; CLU_042258_0_0_9; -.
DR   OMA; PTCGRTQ; -.
DR   OrthoDB; 665306at2; -.
DR   UniPathway; UPA00056; UER00096.
DR   Proteomes; UP000001383; 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   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..371
FT                   /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT                   (flavodoxin)"
FT                   /id="PRO_1000123452"
FT   BINDING         268
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         271
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         303
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         310
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ   SEQUENCE   371 AA;  40001 MW;  A0F521731BCC1DCC CRC64;
     MPEITHRKNT RPVKVGDLTI GGSNELVIQS MTTTKTHDVE ATVAEIKRLE EAGCQIVRVA
     CPKEEDALAI AEIKKQINIP LVVDIHFDYK LALLAIEGGA DKIRINPGNI GRREKVEEVV
     KACKAKGIPI RIGVNAGSLE KHILKKYGYP TADGMVESAL HHIKILEDLD FHDIIVSMKA
     SDVNLAIEAY TKAAQAFDYP LHLGITESGT LFAGTVKSAA GLGAIMSLGI GNTLRISLSA
     DPVEEVKVAR ELLKSFGLAS NAATLISCPT CGRIEIDLIS IANEVEEYIS TIKAPLKVAV
     LGCAVNGPGE AREADIGIAG ARGEGLLFMK GKTVRKVPEE TMVEELKMEI DKLAEEYFKK
     QEAEKLANAE K