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ISPG_RIPO1
ID   ISPG_RIPO1              Reviewed;         406 AA.
AC   B7K5R5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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};
GN   OrderedLocusNames=PCC8801_2798;
OS   Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(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 + 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; CP001287; ACK66798.1; -; Genomic_DNA.
DR   RefSeq; WP_012596064.1; NC_011726.1.
DR   AlphaFoldDB; B7K5R5; -.
DR   SMR; B7K5R5; -.
DR   STRING; 41431.PCC8801_2798; -.
DR   EnsemblBacteria; ACK66798; ACK66798; PCC8801_2798.
DR   KEGG; cyp:PCC8801_2798; -.
DR   eggNOG; COG0821; Bacteria.
DR   HOGENOM; CLU_042258_0_0_3; -.
DR   OMA; PTCGRTQ; -.
DR   OrthoDB; 665306at2; -.
DR   UniPathway; UPA00056; UER00096.
DR   Proteomes; UP000008204; 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; Reference proteome.
FT   CHAIN           1..406
FT                   /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT                   (ferredoxin)"
FT                   /id="PRO_1000118165"
FT   BINDING         315
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         318
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         349
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         356
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ   SEQUENCE   406 AA;  44872 MW;  B51F515855331D32 CRC64;
     MQTLETPKPL TNTSPEFDTT IHRRQTRPVK VGDITIGGGY PVVVQSMINE DTLDIEGSVA
     GIRRLHEIGC EIVRVTVPSM AHAKALAEIN QKLAEVYRRV PLVADVHHNG LKIALEVAKH
     VDKVRINPGL YVFEKPSTTR SEYTQAEFDE IGEKISETLK PLVVSLRDQG KAMRIGVNHG
     SLAERMLFTY GDTPEGMVES ALEFIRICES LDFRNLVISL KASRVPVMLA AYRLMVKRMD
     ELGMDYPLHL GVTEAGDGEY GRIKSTAGIA TLLAEGIGDT IRVSLTEAPE KEIPVCYSIL
     QALGLRKTMV EYVACPSCGR TLFNLEEVLH KVREATKHLT GLDIAVMGCI VNGPGEMADA
     DYGYVGKQAG YISLYRGREE IKRVPEDQGV QELIELIKAD GRWVEP
 
 
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