(data stored in SCRATCH zone)

SWISSPROT: ISPF_BACSU

ID   ISPF_BACSU              Reviewed;         158 AA.
AC   Q06756;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   11-DEC-2019, entry version 134.
DE   RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase;
DE            Short=MECDP-synthase;
DE            Short=MECPP-synthase;
DE            Short=MECPS;
DE            EC=4.6.1.12;
GN   Name=ispF; Synonyms=yacN; OrderedLocusNames=BSU00910;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7510287;
RA   Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M.,
RA   Lapointe J.;
RT   "Clustering and co-transcription of the Bacillus subtilis genes encoding
RT   the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and
RT   the first enzyme for cysteine biosynthesis.";
RL   J. Biol. Chem. 269:7473-7482(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
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   [5]
RP   FUNCTION IN THE ISOPRENE BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RX   PubMed=17458547; DOI=10.1007/s00253-007-0953-5;
RA   Julsing M.K., Rijpkema M., Woerdenbag H.J., Quax W.J., Kayser O.;
RT   "Functional analysis of genes involved in the biosynthesis of isoprene in
RT   Bacillus subtilis.";
RL   Appl. Microbiol. Biotechnol. 75:1377-1384(2007).
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). {ECO:0000269|PubMed:17458547}.
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000250};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 4/6.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene reveal a loss of rod
CC       shape, irregular septation, multicompartmentalized cells, and thickened
CC       cell walls. It also induces a decrease in isoprene production.
CC       {ECO:0000269|PubMed:12270818, ECO:0000269|PubMed:17458547}.
CC   -!- SIMILARITY: Belongs to the IspF family. {ECO:0000305}.
DR   EMBL; L14580; AAA21795.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05325.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11867.1; -; Genomic_DNA.
DR   PIR; F69741; F69741.
DR   RefSeq; NP_387972.1; NC_000964.3.
DR   RefSeq; WP_003225745.1; NZ_JNCM01000029.1.
DR   PDB; 5IWX; X-ray; 1.99 A; A/B/C/D/E/F=1-158.
DR   PDB; 5IWY; X-ray; 1.99 A; A/B/C/D/E/F=1-158.
DR   PDBsum; 5IWX; -.
DR   PDBsum; 5IWY; -.
DR   SMR; Q06756; -.
DR   STRING; 224308.BSU00910; -.
DR   PaxDb; Q06756; -.
DR   PRIDE; Q06756; -.
DR   EnsemblBacteria; CAB11867; CAB11867; BSU00910.
DR   GeneID; 936634; -.
DR   KEGG; bsu:BSU00910; -.
DR   PATRIC; fig|224308.179.peg.92; -.
DR   eggNOG; ENOG4108UH8; Bacteria.
DR   eggNOG; COG0245; LUCA.
DR   HOGENOM; HOG000239175; -.
DR   InParanoid; Q06756; -.
DR   KO; K01770; -.
DR   OMA; PEWSGAS; -.
DR   PhylomeDB; Q06756; -.
DR   BioCyc; BSUB:BSU00910-MONOMER; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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   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;
DR   PRODOM; Q06756.
DR   SWISS-2DPAGE; Q06756.
KW   3D-structure; Isoprene biosynthesis; Lyase; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..158
FT                   /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT                   synthase"
FT                   /id="PRO_0000189441"
FT   REGION          9..11
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          35..36
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          39..47
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          57..59
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          62..66
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          101..107
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          132..136
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   METAL           9
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000250"
FT   METAL           11
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000250"
FT   METAL           43
FT                   /note="Divalent metal cation"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            35
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            134
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   STRAND          2..17
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          19..21
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          24..26
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          29..32
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          34..36
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   HELIX           40..52
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   HELIX           58..61
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   TURN            67..71
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   HELIX           74..87
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          90..100
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          102..104
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   TURN            107..109
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   HELIX           110..120
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   HELIX           125..127
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          128..133
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   HELIX           139..142
FT                   /evidence="ECO:0000244|PDB:5IWX"
FT   STRAND          145..157
FT                   /evidence="ECO:0000244|PDB:5IWX"
SQ   SEQUENCE   158 AA;  17126 MW;  ED11D03EC3752BD0 CRC64;
     MFRIGQGFDV HQLVEGRPLI IGGIEIPYEK GLLGHSDADV LLHTVADACL GAVGEGDIGK
     HFPDTDPEFK DADSFKLLQH VWGIVKQKGY VLGNIDCTII AQKPKMLPYI EDMRKRIAEG
     LEADVSQVNV KATTTEKLGF TGRAEGIAAQ ATVLIQKG
//

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