(data stored in ACNUC1104 zone)

SWISSPROT: A4F6W4_SACEN

ID   A4F6W4_SACEN            Unreviewed;       158 AA.
AC   A4F6W4;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 99.
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:SAAS01078175};
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:SAAS01078202};
GN   Name=ispF {ECO:0000256|HAMAP-Rule:MF_00107,
GN   ECO:0000313|EMBL:CAL99788.1};
GN   OrderedLocusNames=SACE_0440 {ECO:0000313|EMBL:CAL99788.1};
GN   ORFNames=A8924_0837 {ECO:0000313|EMBL:PFG93590.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99788.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99788.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99788.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93590.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93590.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:SAAS01078181}.
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;
CC         EC=4.6.1.12; Evidence={ECO:0000256|HAMAP-Rule:MF_00107,
CC         ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS01115720};
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:SAAS01078193}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00107,
CC       ECO:0000256|SAAS:SAAS01078180}.
CC   -!- SIMILARITY: Belongs to the IspF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00107, ECO:0000256|RuleBase:RU004395,
CC       ECO:0000256|SAAS:SAAS01078179}.
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; AM420293; CAL99788.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93590.1; -; Genomic_DNA.
DR   RefSeq; WP_009947445.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0440; -.
DR   EnsemblBacteria; CAL99788; CAL99788; SACE_0440.
DR   KEGG; sen:SACE_0440; -.
DR   eggNOG; ENOG4108UH8; Bacteria.
DR   eggNOG; COG0245; LUCA.
DR   HOGENOM; HOG000239175; -.
DR   KO; K01770; -.
DR   OMA; DIGHYFP; -.
DR   OrthoDB; 1716560at2; -.
DR   BioCyc; SERY405948:SACE_RS02165-MONOMER; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; A4F6W4.
DR   SWISS-2DPAGE; A4F6W4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00107,
KW   ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS01078191};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395,
KW   ECO:0000256|SAAS:SAAS01078177, ECO:0000313|EMBL:CAL99788.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00107,
KW   ECO:0000256|SAAS:SAAS01078178};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN        4    153       YgbB. {ECO:0000259|Pfam:PF02542}.
FT   REGION       10     12       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       36     37       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       40     48       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       58     60       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION      130    134       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   METAL        10     10       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        12     12       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        44     44       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING      67     67       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00107}.
FT   SITE         36     36       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   SITE        132    132       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
SQ   SEQUENCE   158 AA;  16033 MW;  1C8B90DE3A3411F0 CRC64;
     MIPRIGQGVD VHPVEAGREC WVAGLLWPGE DGCAGHSDGD VASHALCDAL LSAAGLGDLG
     AVFGTGDDRW AGAHGAELLT EARRRVTEAG FGIGNAVVQV VGNRPRIGKR REEAQRVLSE
     VVGAPVSVSG TTTDGLGLTG RGEGIAAVAT ALVFPVES
//

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