ISPG1_STRCO
ID ISPG1_STRCO Reviewed; 384 AA.
AC Q9X7W2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00159};
GN Name=ispG1 {ECO:0000255|HAMAP-Rule:MF_00159}; Synonyms=gcpE, ispG;
GN OrderedLocusNames=SCO6767; ORFNames=SC6A5.16;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP 3D-STRUCTURE MODELING OF 271-375.
RX PubMed=14997523; DOI=10.1002/cbic.200300743;
RA Brandt W., Dessoy M.A., Fulhorst M., Gao W., Zenk M.H., Wessjohann L.A.;
RT "A proposed mechanism for the reductive ring opening of the
RT cyclodiphosphate MEcPP, a crucial transformation in the new DXP/MEP pathway
RT to isoprenoids based on modeling studies and feeding experiments.";
RL ChemBioChem 5:311-323(2004).
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; AL939129; CAB39700.1; -; Genomic_DNA.
DR PIR; T35407; T35407.
DR RefSeq; NP_630839.1; NC_003888.3.
DR RefSeq; WP_011031167.1; NZ_VNID01000002.1.
DR AlphaFoldDB; Q9X7W2; -.
DR SMR; Q9X7W2; -.
DR STRING; 100226.SCO6767; -.
DR GeneID; 1102206; -.
DR KEGG; sco:SCO6767; -.
DR PATRIC; fig|100226.15.peg.6876; -.
DR eggNOG; COG0821; Bacteria.
DR HOGENOM; CLU_042258_0_0_11; -.
DR InParanoid; Q9X7W2; -.
DR OMA; MRIAEQM; -.
DR PhylomeDB; Q9X7W2; -.
DR UniPathway; UPA00056; UER00096.
DR Proteomes; UP000001973; 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; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central.
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..384
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (flavodoxin) 1"
FT /id="PRO_0000190635"
FT BINDING 281
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 284
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 323
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ SEQUENCE 384 AA; 40594 MW; 62D8EA4CF30DBC32 CRC64;
MTAIPLGLPG VPVRPIAERR VSRRIQVGPV AVGGGAPVSV QSMTTTRTSD IGATLQQIAE
LTASGCQIVR VACPTQDDAD ALPVIARKSQ IPVIADIHFQ PKYVFAAIEA GCAAVRVNPG
NIKQFDDKVK EIAKAAKDHG TPIRIGVNAG SLDRRLLQKY GRATPEALAE SALWEASLFE
EHDFRDIKIS VKHNDPVVMV EAYRQLAAQC DYPLHLGVTE AGPAFQGTIK SAVAFGALLS
QGIGDTIRVS LSTPPVEEIK VGIQILESLN LRQRGLEIVS CPSCGRAQVD VYKLAEEVTA
GLEGMEVPLR VAVMGCVVNG PGEAREADLG VASGNGKGQI FVKGEVVKTV PESKIVETLI
EEAMRIAEQM EKDGASGAPA VTVS
