ID D5EEX2_AMICL Unreviewed; 395 AA.
AC D5EEX2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|ARBA:ARBA00012579, ECO:0000256|HAMAP-Rule:MF_00107};
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|ARBA:ARBA00012579, ECO:0000256|HAMAP-Rule:MF_00107};
GN Name=ispF {ECO:0000256|HAMAP-Rule:MF_00107};
GN OrderedLocusNames=Amico_0979 {ECO:0000313|EMBL:ADE57104.1};
OS Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Aminobacterium.
OX NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE57104.1, ECO:0000313|Proteomes:UP000002366};
RN [1] {ECO:0000313|EMBL:ADE57104.1, ECO:0000313|Proteomes:UP000002366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX PubMed=21304712;
RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT 1).";
RL Stand. Genomic Sci. 2:280-289(2010).
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:0000256|HAMAP-Rule:MF_00107}.
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:0000256|ARBA:ARBA00000200, ECO:0000256|HAMAP-
CC Rule:MF_00107, ECO:0000256|RuleBase:RU004395};
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. {ECO:0000256|HAMAP-
CC Rule:MF_00107};
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:0000256|ARBA:ARBA00004709, ECO:0000256|HAMAP-
CC Rule:MF_00107}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00107}.
CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000256|HAMAP-
CC Rule:MF_00107, ECO:0000256|RuleBase:RU004395}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00107}.
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DR EMBL; CP001997; ADE57104.1; -; Genomic_DNA.
DR RefSeq; WP_013048367.1; NC_014011.1.
DR AlphaFoldDB; D5EEX2; -.
DR STRING; 572547.Amico_0979; -.
DR KEGG; aco:Amico_0979; -.
DR eggNOG; COG0245; Bacteria.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_042800_2_5_0; -.
DR OrthoDB; 9806837at2; -.
DR UniPathway; UPA00056; UER00095.
DR Proteomes; UP000002366; Chromosome.
DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070567; F:cytidylyltransferase activity; IEA:InterPro.
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; cd02516; CDP-ME_synthetase; 1.
DR CDD; cd00554; MECDP_synthase; 1.
DR Gene3D; 3.30.1330.50; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; 1.
DR HAMAP; MF_00107; IspF; 1.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR018294; ISPD_synthase_CS.
DR InterPro; IPR003526; MECDP_synthase.
DR InterPro; IPR020555; MECDP_synthase_CS.
DR InterPro; IPR036571; MECDP_synthase_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR00151; ispF; 1.
DR PANTHER; PTHR43181; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43181:SF1; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF02542; YgbB; 1.
DR SUPFAM; SSF69765; IpsF-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS01295; ISPD; 1.
DR PROSITE; PS01350; ISPF; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00107};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00107};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00107}; Reference proteome {ECO:0000313|Proteomes:UP000002366}.
FT DOMAIN 232..387
FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02542"
FT BINDING 238..240
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT BINDING 238
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT BINDING 240
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT BINDING 264..265
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT BINDING 272
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT BINDING 286..288
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT SITE 264
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT SITE 366
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
SQ SEQUENCE 395 AA; 43481 MW; 108503563147573A CRC64;
MKRFSFIIVA AGLGERMGGS PKQFRRLGGK PLWQWSFFTA WELFKKKAIH EIVLVVPLFA
VEQIRKEVAV LSGSSQNCTV TAGGLSRTES VRNGLKGAGC EYVLVHDAAR PFLSVNLCHR
IIEAMDSECG VIPVLPITDA LKKVETIQNQ EAILSLSREN LYITQTPQAF PRCGLLTVLK
GEDDSYRDEA EAWLKFKGSL KKVEGDSFNM KITYPQDFQM AEMLMGNKKE YRTGQGFDIH
PLTPSRILVL GGVTIDSPLG LEGHSDGDVI THAVMDALLG AAGLPDIGIL FPASEPSYKD
AYSFDLLKEV ATLLQRDRWN IEWVDVTLQA QVPPLASYID VIVEKLQSGL CHCGDKKLIV
HLKVKSGELI GPVGNAQCMI CTATATLSRN GRFNE
//
