ID E7A9Z9_HELFC Unreviewed; 361 AA. AC E7A9Z9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000256|HAMAP-Rule:MF_00159}; DE EC=1.17.7.3 {ECO:0000256|HAMAP-Rule:MF_00159}; DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00159}; GN Name=gcpE {ECO:0000313|EMBL:CBY83418.1}; GN Synonyms=ispG {ECO:0000256|HAMAP-Rule:MF_00159}; GN OrderedLocusNames=Hfelis_13340 {ECO:0000313|EMBL:CBY83418.1}; OS Helicobacter felis (strain ATCC 49179 / NCTC 12436 / CS1). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=936155 {ECO:0000313|EMBL:CBY83418.1, ECO:0000313|Proteomes:UP000007934}; RN [1] {ECO:0000313|Proteomes:UP000007934} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49179 / NCTC 12436 / CS1 RC {ECO:0000313|Proteomes:UP000007934}; RA Arnold A., Zigova Z., Lawley T., Falkow S., Bentley S., Aslett M., RA Muller A.; RT "Comparative whole genome analysis of the carcinogenic bacterial pathogen RT Helicobacter felis."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBY83418.1, ECO:0000313|Proteomes:UP000007934} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49179 / NCTC 12436 / CS1 RC {ECO:0000313|Proteomes:UP000007934}; RX PubMed=21402865; RA Arnold I.C., Zigova Z., Holden M., Lawley T.D., Rad R., Dougan G., RA Falkow S., Bentley S.D., Muller A.; RT "Comparative whole genome sequence analysis of the carcinogenic bacterial RT model pathogen Helicobacter felis."; RL Genome Biol. Evol. 3:302-308(2011). CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate CC (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00159}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00159}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00159}. CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000256|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; FQ670179; CBY83418.1; -; Genomic_DNA. DR RefSeq; WP_013469782.1; NC_014810.2. DR AlphaFoldDB; E7A9Z9; -. DR STRING; 936155.HFELIS_13340; -. DR GeneID; 36133317; -. DR KEGG; hfe:HFELIS_13340; -. DR eggNOG; COG0821; Bacteria. DR HOGENOM; CLU_042258_0_0_7; -. DR OrthoDB; 9803214at2; -. DR UniPathway; UPA00056; UER00096. DR Proteomes; UP000007934; 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; Dihydropteroate synthase-like; 1. DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1. DR HAMAP; MF_00159; IspG; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like_sf. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR016425; IspG_bac. DR InterPro; IPR004588; IspG_bac-typ. DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf. DR NCBIfam; TIGR00612; ispG_gcpE; 1. DR PANTHER; PTHR30454; 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR30454:SF0; 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE (FERREDOXIN), CHLOROPLASTIC; 1. DR Pfam; PF04551; GcpE; 1. DR PIRSF; PIRSF004640; IspG; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00159}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00159}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00159}; KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP- KW Rule:MF_00159}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00159}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00159}; Reference proteome {ECO:0000313|Proteomes:UP000007934}. FT BINDING 263 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159" FT BINDING 266 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159" FT BINDING 298 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159" FT BINDING 305 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159" SQ SEQUENCE 361 AA; 39262 MW; 2F1C03877B676EB3 CRC64; MHPRFPTQQI SIGHVLIGGD APISTQSMTF SQTCDIEATK AQIDRLKLAG ADLVRVAVRH KKDALALKEL KKVASLPLIA DIHFHHHLAL IAAESVDAIR INPGNIGAPE KIKAVAQACN ARNLPIRIGV NGGSLEKPFE LKYGATPEGM VQSALYNIKF LEDAGFTNIK ISLKASDVER TIAAYQQLRP LVPYPFHLGV TEAGSLFHSS IKSAMALGQL LREGIGDTMR VSITGELEEE IRVAKAILRY SGRQKEGITF ISCPTCGRIE SNLVAMMSQV EQRLAHIKIP LDVSVMGCVV NALGEAKHAD IAIAFGKKSG LIIKKGKVIH KLPEDQLLET FVTEVQTLAL EQQKEDIHAK I //