ISPG_BACAN
ID ISPG_BACAN Reviewed; 367 AA.
AC Q81LV7; Q6HTA9; Q6KMK1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
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}; Synonyms=gcpE;
GN OrderedLocusNames=BA_4502, GBAA_4502, BAS4180;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAT56480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016879; AAP28213.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33621.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56480.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_846727.1; NC_003997.3.
DR RefSeq; WP_002194540.1; NZ_WXXJ01000027.1.
DR PDB; 4MWA; X-ray; 1.85 A; A/B/C/D/E/F/G/H=1-270.
DR PDBsum; 4MWA; -.
DR AlphaFoldDB; Q81LV7; -.
DR SMR; Q81LV7; -.
DR STRING; 260799.BAS4180; -.
DR DNASU; 1088122; -.
DR EnsemblBacteria; AAP28213; AAP28213; BA_4502.
DR EnsemblBacteria; AAT33621; AAT33621; GBAA_4502.
DR GeneID; 45024158; -.
DR KEGG; ban:BA_4502; -.
DR KEGG; bar:GBAA_4502; -.
DR KEGG; bat:BAS4180; -.
DR PATRIC; fig|198094.11.peg.4470; -.
DR eggNOG; COG0821; Bacteria.
DR HOGENOM; CLU_042258_0_0_9; -.
DR UniPathway; UPA00056; UER00096.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; SSF51717; SSF51717; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR00612; ispG_gcpE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..367
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (flavodoxin)"
FT /id="PRO_0000190527"
FT BINDING 265
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 268
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 300
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT BINDING 307
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:4MWA"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 180..193
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 208..224
FT /evidence="ECO:0007829|PDB:4MWA"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4MWA"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:4MWA"
SQ SEQUENCE 367 AA; 39653 MW; C6FC99772B9D9C17 CRC64;
MTHRTKTRPV KVGNLTIGGN NELIIQSMTT TKTHDVEATV AEIKRLEEAG CQVVRVAVPD
ERAANAIADI KKQINIPLVA DIHFDYRLAL KAIEGGIDKV RINPGNIGRR HKVEAVVNAA
KERGIPIRIG VNAGSLERHI LEKYGYPTAD GMVESALHHI KILEDLDFHD IIVSMKASDV
NLAIEAYEKA ARAFDYPLHL GITESGTLFA GTVKSAAGLG AILNKGIGNT LRISLSADPV
EEVKVARELL KSFGLASNAA TLISCPTCGR IEIDLISIAN EVEEYISTLQ VPIKVAVLGC
AVNGPGEARE ADIGIAGARG EGLLFRKGQV VRKVPEEIMV EELKKEIDVI AAEMAAEREK
EKETQEQ
