ID   ISPG_NEIM0              Reviewed;         421 AA.
AC   A9LZN8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=NMCC_1223;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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; CP000381; ABX73396.1; -; Genomic_DNA.
DR   RefSeq; WP_002232580.1; NC_010120.1.
DR   AlphaFoldDB; A9LZN8; -.
DR   SMR; A9LZN8; -.
DR   EnsemblBacteria; ABX73396; ABX73396; NMCC_1223.
DR   KEGG; nmn:NMCC_1223; -.
DR   HOGENOM; CLU_042258_1_0_4; -.
DR   OMA; PTCGRTQ; -.
DR   UniPathway; UPA00056; UER00096.
DR   Proteomes; UP000001177; 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; 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.
FT   CHAIN           1..421
FT                   /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT                   (flavodoxin)"
FT                   /id="PRO_1000076890"
FT   BINDING         298
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         301
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         344
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         351
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ   SEQUENCE   421 AA;  45373 MW;  C80BE86C8FD5A12D CRC64;
     MNTLQRRKTH QVRIDHITVG SEAPVVIQSM TNTDTADAKA TALQIKELSD AGSEMVRITV
     NSPEAASKVA EIRRRLDDMG YATPLIGDFH FNGERLLAEF PECGKALSKY RINPGNVGKG
     VKGDEKFAFM IRTAAENDKA VRIGVNWGSL DQSLAKRMMD ANLASSAPKP PEEVTKEALI
     VSALESAEKA VLLGLPEDKI ILSCKVSAVQ DLIQVYRELG SRCAYPLHLG LTEAGMGSKG
     IVASTAALSV LLQEGIGDTI RISLTPEPGS PRTQEVVVGQ EILQTMGLRS FTPMVTACPG
     CGRTTSTVFQ ELAQDVQNYL RQKMSIWRTL YPGVESLNVA VMGCVVNGPG ESKLADIGIS
     LPGTGETPVA PVYVDGERKV TLKGDNIATE FLAIVEEYVK TNYGENGSKR NQNKIIPIQS
     L