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ISPG_CHLTB
ID   ISPG_CHLTB              Reviewed;         602 AA.
AC   B0BB44;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=CTLon_0308;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(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}.
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DR   EMBL; AM884177; CAP06706.1; -; Genomic_DNA.
DR   RefSeq; WP_012263592.1; NC_010280.2.
DR   AlphaFoldDB; B0BB44; -.
DR   KEGG; ctl:CTLon_0308; -.
DR   HOGENOM; CLU_012689_0_0_0; -.
DR   OMA; YGYVGAG; -.
DR   UniPathway; UPA00056; UER00096.
DR   Proteomes; UP000000794; 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; IPR017178; IspG_atypical.
DR   InterPro; IPR004588; IspG_bac-typ.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   PANTHER; PTHR30454; PTHR30454; 1.
DR   Pfam; PF04551; GcpE; 2.
DR   PIRSF; PIRSF037336; IspG_like; 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..602
FT                   /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT                   (flavodoxin)"
FT                   /id="PRO_1000097155"
FT   BINDING         508
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         511
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         543
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         550
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ   SEQUENCE   602 AA;  66607 MW;  62D2A6DD986120A5 CRC64;
     MATPCIQNAF RRKTLPVRIG DLFVGSEHSI KIQSMTTTAT TDVDGTVRQI CALQEWGCDI
     VRVTVQGLRE VHACEHIKDR LIQQNISIPL VADIHFFPQA AIHVVDCVDK VRINPGNYVD
     KRNMFTGKIY SDEQYAHSLE HLMNKFSPLV EKCKRLGKAM RIGVNHGSLS ERVTQRYGNT
     IEGMVYSALE YAEVCVAMDY HDVIFSMKSS NPKVMVAAYR SLAYELDQRE WSYPLHLGVT
     EAGSGTAGIV KSAVGIGTLL SEGLGDTIRC SLTGSPINEI PICIDLLKQT TELSERWGEA
     DNPFAIHSSK QLGTRNTLNT PPWGNVYGLL INLTDVQLLT AEPIELLQCL GIDTTTGKID
     PTTPEGVVVP KAMRSSPIVS EIEKHLLVFN KEDAPILNPM NEEEWLSEET LSAPFVYFEV
     TDIHTARRFF SLRQHSTQPV CLSFSLDPHL SKNEAIIDLS ARLGALLLDG LGSCVLLDFV
     DIKLSRTLGF LILQSANIRS VTVEYVSCPG CGRTLFDLLA VSQRIRERTK HLPGGLKIAV
     MGCIVNGPGE MADADFGYVG SKPGMIDLYV KHKCVKSCIP IENAEEELVQ LLKEHGVWKE
     PE
 
 
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