ISPF_ECOLI
ID ISPF_ECOLI Reviewed; 159 AA.
AC P62617; P36663; Q2MA83;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00107};
DE Short=MECDP-synthase {ECO:0000255|HAMAP-Rule:MF_00107};
DE Short=MECPP-synthase {ECO:0000255|HAMAP-Rule:MF_00107};
DE Short=MECPS {ECO:0000255|HAMAP-Rule:MF_00107};
DE EC=4.6.1.12 {ECO:0000255|HAMAP-Rule:MF_00107, ECO:0000269|PubMed:10694574, ECO:0000269|PubMed:22839733};
GN Name=ispF {ECO:0000255|HAMAP-Rule:MF_00107}; Synonyms=mecS, ygbB;
GN OrderedLocusNames=b2746, JW2716;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MP180;
RX PubMed=7928962; DOI=10.1128/jb.176.19.6015-6022.1994;
RA Li C., Ichikawa J.K., Ravetto J.J., Kuo H.-C., Fu J.C., Clarke S.;
RT "A new gene involved in stationary-phase survival located at 59 minutes on
RT the Escherichia coli chromosome.";
RL J. Bacteriol. 176:6015-6022(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN
RP MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND COFACTOR.
RX PubMed=10694574; DOI=10.1073/pnas.040554697;
RA Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S.,
RA Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.;
RT "Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-
RT methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-
RT cyclodiphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RA Takagi M., Kuzuyama T., Kaneda K., Watanabe H., Dairi T., Seto H.;
RT "Studies on the nonmevalonate pathway: formation of 2-C-methyl-D-erythritol
RT 2,4-cyclodiphosphate from 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-
RT erythritol.";
RL Tetrahedron Lett. 41:3395-3398(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=12270818; DOI=10.1128/jb.184.20.5609-5618.2002;
RA Campbell T.L., Brown E.D.;
RT "Characterization of the depletion of 2-C-methyl-D-erythritol-2,4-
RT cyclodiphosphate synthase in Escherichia coli and Bacillus subtilis.";
RL J. Bacteriol. 184:5609-5618(2002).
RN [8]
RP FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22839733; DOI=10.1021/cb300243w;
RA Bitok J.K., Meyers C.F.;
RT "2C-Methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate
RT synthase IspF activity.";
RL ACS Chem. Biol. 7:1702-1710(2012).
RN [9] {ECO:0007744|PDB:1KNJ, ECO:0007744|PDB:1KNK}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND
RP DIVALENT CATIONS, COFACTOR, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=11786530; DOI=10.1074/jbc.c100739200;
RA Richard S.B., Ferrer J.-L., Bowman M.E., Lillo A.M., Tetzlaff C.N.,
RA Cane D.E., Noel J.P.;
RT "Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
RT synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic
RT pathway.";
RL J. Biol. Chem. 277:8667-8672(2002).
RN [10] {ECO:0007744|PDB:1JY8, ECO:0007744|PDB:1U3L, ECO:0007744|PDB:1U3P, ECO:0007744|PDB:1U40, ECO:0007744|PDB:1U43}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND
RP DIVALENT CATIONS, MUTAGENESIS OF ASP-8; HIS-42 AND ASP-56, COFACTOR, AND
RP SUBUNIT.
RX PubMed=11829504; DOI=10.1006/jmbi.2001.5341;
RA Steinbacher S., Kaiser J., Wungsintaweekul J., Hecht S., Eisenreich W.,
RA Gerhardt S., Bacher A., Rohdich F.;
RT "Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved
RT in mevalonate-independent biosynthesis of isoprenoids.";
RL J. Mol. Biol. 316:79-88(2002).
RN [11] {ECO:0007744|PDB:1GX1}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND
RP DIVALENT CATIONS, COFACTOR, AND SUBUNIT.
RX PubMed=11997478; DOI=10.1073/pnas.102679799;
RA Kemp L.E., Bond C.S., Hunter W.N.;
RT "Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase: an
RT essential enzyme for isoprenoid biosynthesis and target for antimicrobial
RT drug development.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6591-6596(2002).
RN [12] {ECO:0007744|PDB:1H47, ECO:0007744|PDB:1H48}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND
RP DIVALENT CATIONS, COFACTOR, AND SUBUNIT.
RX PubMed=15608374; DOI=10.1107/s0907444904025971;
RA Kemp L.E., Alphey M.S., Bond C.S., Ferguson M.A., Hecht S., Bacher A.,
RA Eisenreich W., Rohdich F., Hunter W.N.;
RT "The identification of isoprenoids that bind in the intersubunit cavity of
RT Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase by
RT complementary biophysical methods.";
RL Acta Crystallogr. D 61:45-52(2005).
RN [13] {ECO:0007744|PDB:1YQN}
RP X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF DOUBLE MUTANT MET-142/LEU-144 IN
RP COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ARG-142
RP AND GLU-144, AND COFACTOR.
RX PubMed=16511114; DOI=10.1107/s1744309105018762;
RA Sgraja T., Kemp L.E., Ramsden N., Hunter W.N.;
RT "A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-
RT cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to
RT prevent binding of, an isoprenoid diphosphate.";
RL Acta Crystallogr. F 61:625-629(2005).
RN [14] {ECO:0007744|PDB:2AMT, ECO:0007744|PDB:2GZL}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND
RP ZINC IONS, COFACTOR, AND SUBUNIT.
RX PubMed=16392111; DOI=10.1002/anie.200503003;
RA Crane C.M., Kaiser J., Ramsden N.L., Lauw S., Rohdich F., Eisenreich W.,
RA Hunter W.N., Bacher A., Diederich F.;
RT "Fluorescent inhibitors for IspF, an enzyme in the non-mevalonate pathway
RT for isoprenoid biosynthesis and a potential target for antimalarial
RT therapy.";
RL Angew. Chem. Int. Ed. 45:1069-1074(2006).
RN [15] {ECO:0007744|PDB:3ELC, ECO:0007744|PDB:3EOR, ECO:0007744|PDB:3ERN, ECO:0007744|PDB:3ESJ, ECO:0007744|PDB:3FBA}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND
RP ZINC IONS, COFACTOR, AND SUBUNIT.
RX PubMed=19320487; DOI=10.1021/jm801475n;
RA Ramsden N.L., Buetow L., Dawson A., Kemp L.A., Ulaganathan V., Brenk R.,
RA Klebe G., Hunter W.N.;
RT "A structure-based approach to ligand discovery for 2C-methyl-D-erythritol-
RT 2,4-cyclodiphosphate synthase: a target for antimicrobial therapy.";
RL J. Med. Chem. 52:2531-2542(2009).
CC -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP)
CC and dimethylallyl diphosphate (DMAPP), two major building blocks of
CC isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-
CC C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol
CC 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine
CC 5-monophosphate (CMP). Also converts 4-diphosphocytidyl-2-C-methyl-D-
CC erythritol into 2-C-methyl-D-erythritol 3,4-cyclophosphate and CMP.
CC {ECO:0000269|PubMed:10694574, ECO:0000269|PubMed:22839733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-
CC erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00107,
CC ECO:0000269|PubMed:10694574, ECO:0000269|PubMed:22839733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 3,4-
CC cyclophosphate + CMP + H(+); Xref=Rhea:RHEA:68364, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57823, ChEBI:CHEBI:60377, ChEBI:CHEBI:177365;
CC Evidence={ECO:0000269|PubMed:10694574};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00107,
CC ECO:0000269|PubMed:10694574, ECO:0000269|PubMed:11786530,
CC ECO:0000269|PubMed:11829504, ECO:0000269|PubMed:11997478,
CC ECO:0000269|PubMed:15608374, ECO:0000269|PubMed:16392111,
CC ECO:0000269|PubMed:16511114, ECO:0000269|PubMed:19320487};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00107, ECO:0000269|PubMed:10694574,
CC ECO:0000269|PubMed:11786530, ECO:0000269|PubMed:11829504,
CC ECO:0000269|PubMed:11997478, ECO:0000269|PubMed:15608374,
CC ECO:0000269|PubMed:16392111, ECO:0000269|PubMed:16511114,
CC ECO:0000269|PubMed:19320487};
CC -!- ACTIVITY REGULATION: Activated by 2C-methyl-D-erythritol 4-phosphate
CC (MEP). {ECO:0000269|PubMed:22839733}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=339 uM for CDP-ME2P (at pH 7.4) {ECO:0000269|PubMed:22839733};
CC Note=kcat is 61 min(-1) for CDP-ME2P (at pH 7.4).;
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 4/6. {ECO:0000255|HAMAP-Rule:MF_00107}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00107,
CC ECO:0000269|PubMed:11786530, ECO:0000269|PubMed:11829504,
CC ECO:0000269|PubMed:11997478, ECO:0000269|PubMed:15608374,
CC ECO:0000269|PubMed:16392111, ECO:0000269|PubMed:16511114,
CC ECO:0000269|PubMed:19320487}.
CC -!- INTERACTION:
CC P62617; P67910: hldD; NbExp=2; IntAct=EBI-562321, EBI-543760;
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene reveal a filamentous
CC phenotype. {ECO:0000269|PubMed:12270818}.
CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000255|HAMAP-
CC Rule:MF_00107, ECO:0000305}.
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DR EMBL; L07942; AAA79837.1; -; Genomic_DNA.
DR EMBL; AF230738; AAF44656.1; -; Genomic_DNA.
DR EMBL; AB038256; BAA95145.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69256.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75788.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76823.1; -; Genomic_DNA.
DR PIR; I55083; I55083.
DR RefSeq; NP_417226.1; NC_000913.3.
DR RefSeq; WP_001219242.1; NZ_SSUR01000024.1.
DR PDB; 1GX1; X-ray; 1.80 A; A/B/C=1-159.
DR PDB; 1H47; X-ray; 2.00 A; A/B/C/D/E/F=1-159.
DR PDB; 1H48; X-ray; 2.30 A; A/B/C/D/E/F=1-159.
DR PDB; 1JY8; X-ray; 2.50 A; A=1-159.
DR PDB; 1KNJ; X-ray; 2.80 A; A=1-159.
DR PDB; 1KNK; X-ray; 2.80 A; A=1-159.
DR PDB; 1U3L; X-ray; 2.50 A; A=1-159.
DR PDB; 1U3P; X-ray; 2.85 A; A=1-159.
DR PDB; 1U40; X-ray; 2.80 A; A=1-159.
DR PDB; 1U43; X-ray; 3.20 A; A=1-159.
DR PDB; 1YQN; X-ray; 3.11 A; A=1-159.
DR PDB; 2AMT; X-ray; 2.30 A; A/B/C/D/E/F=1-159.
DR PDB; 2GZL; X-ray; 2.50 A; A=1-157.
DR PDB; 3ELC; X-ray; 2.50 A; A/B/C=1-159.
DR PDB; 3EOR; X-ray; 2.90 A; A=1-159.
DR PDB; 3ERN; X-ray; 2.10 A; A/B/C/D/E/F=1-159.
DR PDB; 3ESJ; X-ray; 2.70 A; A=1-159.
DR PDB; 3FBA; X-ray; 3.10 A; A=1-159.
DR PDBsum; 1GX1; -.
DR PDBsum; 1H47; -.
DR PDBsum; 1H48; -.
DR PDBsum; 1JY8; -.
DR PDBsum; 1KNJ; -.
DR PDBsum; 1KNK; -.
DR PDBsum; 1U3L; -.
DR PDBsum; 1U3P; -.
DR PDBsum; 1U40; -.
DR PDBsum; 1U43; -.
DR PDBsum; 1YQN; -.
DR PDBsum; 2AMT; -.
DR PDBsum; 2GZL; -.
DR PDBsum; 3ELC; -.
DR PDBsum; 3EOR; -.
DR PDBsum; 3ERN; -.
DR PDBsum; 3ESJ; -.
DR PDBsum; 3FBA; -.
DR AlphaFoldDB; P62617; -.
DR SMR; P62617; -.
DR BioGRID; 4262279; 277.
DR DIP; DIP-48029N; -.
DR IntAct; P62617; 7.
DR STRING; 511145.b2746; -.
DR BindingDB; P62617; -.
DR ChEMBL; CHEMBL3217375; -.
DR DrugBank; DB02552; Geranyl Diphosphate.
DR jPOST; P62617; -.
DR PaxDb; P62617; -.
DR PRIDE; P62617; -.
DR EnsemblBacteria; AAC75788; AAC75788; b2746.
DR EnsemblBacteria; BAE76823; BAE76823; BAE76823.
DR GeneID; 67413962; -.
DR GeneID; 945057; -.
DR KEGG; ecj:JW2716; -.
DR KEGG; eco:b2746; -.
DR PATRIC; fig|1411691.4.peg.3994; -.
DR EchoBASE; EB1763; -.
DR eggNOG; COG0245; Bacteria.
DR HOGENOM; CLU_084630_2_0_6; -.
DR InParanoid; P62617; -.
DR OMA; QHFGTGR; -.
DR PhylomeDB; P62617; -.
DR BioCyc; EcoCyc:EG11816-MON; -.
DR BioCyc; MetaCyc:EG11816-MON; -.
DR BRENDA; 4.6.1.12; 2026.
DR SABIO-RK; P62617; -.
DR UniPathway; UPA00056; UER00095.
DR EvolutionaryTrace; P62617; -.
DR PRO; PR:P62617; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
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 GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:EcoCyc.
DR CDD; cd00554; MECDP_synthase; 1.
DR Gene3D; 3.30.1330.50; -; 1.
DR HAMAP; MF_00107; IspF; 1.
DR InterPro; IPR003526; MECDP_synthase.
DR InterPro; IPR020555; MECDP_synthase_CS.
DR InterPro; IPR036571; MECDP_synthase_sf.
DR PANTHER; PTHR43181; PTHR43181; 1.
DR Pfam; PF02542; YgbB; 1.
DR SUPFAM; SSF69765; SSF69765; 1.
DR TIGRFAMs; TIGR00151; ispF; 1.
DR PROSITE; PS01350; ISPF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isoprene biosynthesis; Lyase;
KW Metal-binding; Reference proteome.
FT CHAIN 1..159
FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT synthase"
FT /id="PRO_0000189464"
FT BINDING 8..10
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:11829504,
FT ECO:0000269|PubMed:11997478, ECO:0000269|PubMed:15608374,
FT ECO:0000269|PubMed:16392111, ECO:0000269|PubMed:16511114,
FT ECO:0000312|PDB:1U3P, ECO:0007744|PDB:1GX1,
FT ECO:0007744|PDB:1H48, ECO:0007744|PDB:1JY8,
FT ECO:0007744|PDB:1U3L, ECO:0007744|PDB:1U40,
FT ECO:0007744|PDB:1YQN, ECO:0007744|PDB:2AMT"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:11786530,
FT ECO:0000269|PubMed:11829504, ECO:0000269|PubMed:11997478,
FT ECO:0000269|PubMed:15608374, ECO:0000269|PubMed:16392111,
FT ECO:0000269|PubMed:16511114, ECO:0000269|PubMed:19320487,
FT ECO:0007744|PDB:1GX1, ECO:0007744|PDB:1H47,
FT ECO:0007744|PDB:1H48, ECO:0007744|PDB:1JY8,
FT ECO:0007744|PDB:1U3L, ECO:0007744|PDB:1U3P,
FT ECO:0007744|PDB:1U40, ECO:0007744|PDB:1YQN,
FT ECO:0007744|PDB:2AMT, ECO:0007744|PDB:2GZL,
FT ECO:0007744|PDB:3ELC, ECO:0007744|PDB:3EOR,
FT ECO:0007744|PDB:3ERN, ECO:0007744|PDB:3ESJ,
FT ECO:0007744|PDB:3FBA"
FT BINDING 10
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:11786530,
FT ECO:0000269|PubMed:11829504, ECO:0000269|PubMed:11997478,
FT ECO:0000269|PubMed:15608374, ECO:0000269|PubMed:16392111,
FT ECO:0000269|PubMed:16511114, ECO:0000269|PubMed:19320487,
FT ECO:0007744|PDB:1GX1, ECO:0007744|PDB:1H47,
FT ECO:0007744|PDB:1H48, ECO:0007744|PDB:1JY8,
FT ECO:0007744|PDB:1U3L, ECO:0007744|PDB:1U3P,
FT ECO:0007744|PDB:1U40, ECO:0007744|PDB:1YQN,
FT ECO:0007744|PDB:2AMT, ECO:0007744|PDB:2GZL,
FT ECO:0007744|PDB:3ELC, ECO:0007744|PDB:3EOR,
FT ECO:0007744|PDB:3ERN, ECO:0007744|PDB:3ESJ,
FT ECO:0007744|PDB:3FBA"
FT BINDING 34..35
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:11786530,
FT ECO:0000269|PubMed:11829504, ECO:0000269|PubMed:15608374,
FT ECO:0000269|PubMed:16392111, ECO:0007744|PDB:1H48,
FT ECO:0007744|PDB:1KNJ, ECO:0007744|PDB:1U43,
FT ECO:0007744|PDB:2AMT"
FT BINDING 42
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:11786530,
FT ECO:0000269|PubMed:11829504, ECO:0000269|PubMed:11997478,
FT ECO:0000269|PubMed:15608374, ECO:0000269|PubMed:16392111,
FT ECO:0000269|PubMed:16511114, ECO:0000269|PubMed:19320487,
FT ECO:0007744|PDB:1GX1, ECO:0007744|PDB:1H47,
FT ECO:0007744|PDB:1H48, ECO:0007744|PDB:1JY8,
FT ECO:0007744|PDB:1U3L, ECO:0007744|PDB:1U3P,
FT ECO:0007744|PDB:1U40, ECO:0007744|PDB:1YQN,
FT ECO:0007744|PDB:2AMT, ECO:0007744|PDB:2GZL,
FT ECO:0007744|PDB:3ELC, ECO:0007744|PDB:3EOR,
FT ECO:0007744|PDB:3ERN, ECO:0007744|PDB:3ESJ,
FT ECO:0007744|PDB:3FBA"
FT BINDING 56..58
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:11829504,
FT ECO:0000269|PubMed:11997478, ECO:0000269|PubMed:15608374,
FT ECO:0000269|PubMed:16392111, ECO:0000269|PubMed:16511114,
FT ECO:0000269|PubMed:19320487, ECO:0000312|PDB:1U43,
FT ECO:0007744|PDB:1GX1, ECO:0007744|PDB:1H48,
FT ECO:0007744|PDB:1U3L, ECO:0007744|PDB:1U3P,
FT ECO:0007744|PDB:1YQN, ECO:0007744|PDB:2AMT,
FT ECO:0007744|PDB:2GZL, ECO:0007744|PDB:3ERN"
FT BINDING 61..65
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:11829504,
FT ECO:0000269|PubMed:15608374, ECO:0000312|PDB:1JY8,
FT ECO:0007744|PDB:1H48, ECO:0007744|PDB:1U3P,
FT ECO:0007744|PDB:1U40"
FT BINDING 100..106
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:11786530,
FT ECO:0000269|PubMed:11997478, ECO:0000269|PubMed:15608374,
FT ECO:0000269|PubMed:16392111, ECO:0000269|PubMed:19320487,
FT ECO:0007744|PDB:1GX1, ECO:0007744|PDB:1H48,
FT ECO:0007744|PDB:1KNJ, ECO:0007744|PDB:1U3L,
FT ECO:0007744|PDB:1YQN, ECO:0007744|PDB:2AMT,
FT ECO:0007744|PDB:3ELC, ECO:0007744|PDB:3EOR,
FT ECO:0007744|PDB:3ERN, ECO:0007744|PDB:3ESJ,
FT ECO:0007744|PDB:3FBA"
FT BINDING 132..135
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:11997478,
FT ECO:0000269|PubMed:15608374, ECO:0000269|PubMed:16392111,
FT ECO:0000269|PubMed:19320487, ECO:0007744|PDB:1GX1,
FT ECO:0007744|PDB:1H48, ECO:0007744|PDB:1U3L,
FT ECO:0007744|PDB:1YQN, ECO:0007744|PDB:2AMT,
FT ECO:0007744|PDB:3ERN"
FT BINDING 139
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:15608374,
FT ECO:0000269|PubMed:16392111, ECO:0000269|PubMed:16511114,
FT ECO:0000269|PubMed:19320487, ECO:0007744|PDB:1H48,
FT ECO:0007744|PDB:1YQN, ECO:0007744|PDB:2AMT,
FT ECO:0007744|PDB:3ELC, ECO:0007744|PDB:3ERN"
FT BINDING 142
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000269|PubMed:15608374,
FT ECO:0000269|PubMed:16392111, ECO:0000269|PubMed:19320487,
FT ECO:0000312|PDB:3ELC, ECO:0007744|PDB:1H48,
FT ECO:0007744|PDB:2AMT, ECO:0007744|PDB:2GZL,
FT ECO:0007744|PDB:3EOR, ECO:0007744|PDB:3ERN,
FT ECO:0007744|PDB:3ESJ, ECO:0007744|PDB:3FBA"
FT SITE 34
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107,
FT ECO:0000305|PubMed:11786530"
FT SITE 133
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107,
FT ECO:0000305|PubMed:11786530"
FT MUTAGEN 8
FT /note="D->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11829504"
FT MUTAGEN 42
FT /note="H->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11829504"
FT MUTAGEN 56
FT /note="D->S: 35% decrease of activity."
FT /evidence="ECO:0000269|PubMed:11829504"
FT MUTAGEN 142
FT /note="R->M: Little effect on the overall structure; when
FT associated with L-144."
FT /evidence="ECO:0000269|PubMed:16511114"
FT MUTAGEN 144
FT /note="E->L: Little effect on the overall structure; when
FT associated with M-142."
FT /evidence="ECO:0000269|PubMed:16511114"
FT STRAND 1..16
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1GX1"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1GX1"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1U43"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2GZL"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1GX1"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1GX1"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:1GX1"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1GX1"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1GX1"
FT STRAND 144..155
FT /evidence="ECO:0007829|PDB:1GX1"
SQ SEQUENCE 159 AA; 16898 MW; 9FC5563623A62939 CRC64;
MRIGHGFDVH AFGGEGPIII GGVRIPYEKG LLAHSDGDVA LHALTDALLG AAALGDIGKL
FPDTDPAFKG ADSRELLREA WRRIQAKGYT LGNVDVTIIA QAPKMLPHIP QMRVFIAEDL
GCHMDDVNVK ATTTEKLGFT GRGEGIACEA VALLIKATK
