(data stored in SCRATCH zone)

SWISSPROT: C6WGL5_ACTMD

ID   C6WGL5_ACTMD            Unreviewed;       155 AA.
AC   C6WGL5;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS00731908};
DE            Short=MECDP-synthase {ECO:0000256|HAMAP-Rule:MF_00107};
DE            Short=MECPP-synthase {ECO:0000256|HAMAP-Rule:MF_00107};
DE            Short=MECPS {ECO:0000256|HAMAP-Rule:MF_00107};
DE            EC=4.6.1.12 {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS00771960};
GN   Name=ispF {ECO:0000256|HAMAP-Rule:MF_00107};
GN   OrderedLocusNames=Amir_0362 {ECO:0000313|EMBL:ACU34331.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34331.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34331.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate
CC       (IPP) and dimethylallyl diphosphate (DMAPP), two major building
CC       blocks of isoprenoid compounds. Catalyzes the conversion of 4-
CC       diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to
CC       2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a
CC       corresponding release of cytidine 5-monophosphate (CMP).
CC       {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|SAAS:SAAS00731896}.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C-
CC       methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
CC       + CMP. {ECO:0000256|HAMAP-Rule:MF_00107,
CC       ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS00771955}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00107};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00107};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00107, ECO:0000256|SAAS:SAAS00771963}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00107,
CC       ECO:0000256|SAAS:SAAS00771974}.
CC   -!- SIMILARITY: Belongs to the IspF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00107, ECO:0000256|RuleBase:RU004395,
CC       ECO:0000256|SAAS:SAAS00771990}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00107}.
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DR   EMBL; CP001630; ACU34331.1; -; Genomic_DNA.
DR   RefSeq; WP_012782994.1; NC_013093.1.
DR   STRING; 446462.Amir_0362; -.
DR   EnsemblBacteria; ACU34331; ACU34331; Amir_0362.
DR   KEGG; ami:Amir_0362; -.
DR   eggNOG; ENOG4108UH8; Bacteria.
DR   eggNOG; COG0245; LUCA.
DR   HOGENOM; HOG000239175; -.
DR   KO; K01770; -.
DR   OMA; DIGHYFP; -.
DR   OrthoDB; POG091H023X; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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   Pfam; PF02542; YgbB; 1.
DR   SUPFAM; SSF69765; SSF69765; 1.
DR   TIGRFAMs; TIGR00151; ispF; 1.
DR   PROSITE; PS01350; ISPF; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGL5.
DR   SWISS-2DPAGE; C6WGL5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00107,
KW   ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS00771928};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395,
KW   ECO:0000256|SAAS:SAAS00771989, ECO:0000313|EMBL:ACU34331.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00107,
KW   ECO:0000256|SAAS:SAAS00771962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN        1    151       YgbB. {ECO:0000259|Pfam:PF02542}.
FT   REGION        8     10       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       34     35       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       38     46       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       56     58       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION      128    132       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   METAL         8      8       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        10     10       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        42     42       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING      65     65       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING     139    139       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00107}.
FT   SITE         34     34       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   SITE        130    130       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
SQ   SEQUENCE   155 AA;  15536 MW;  58EC6DE369E6490A CRC64;
     MRVGIGTDVH PVEPGRDCWM VGLLWEGADG CAGHSDGDVA AHALCDALLS AAGLGDLGAV
     FGTSDPRWSG AHGVEFLAEA RRLVEAEGFV VGNAAVQVIG NAPRVGKRRA EAQKVLSEVL
     GGPVSVSGTT TDGLGLTGRG EGVAAVATAL LLPKG
//

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