GenomeNet

Database: UniProt
Entry: J4V4T3_9GAMM
LinkDB: J4V4T3_9GAMM
Original site: J4V4T3_9GAMM 
ID   J4V4T3_9GAMM            Unreviewed;       381 AA.
AC   J4V4T3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
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   ORFNames=NT02SARS_0343 {ECO:0000313|EMBL:EJP73512.1};
OS   SAR86 cluster bacterium SAR86B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX   NCBI_TaxID=1123867 {ECO:0000313|EMBL:EJP73512.1, ECO:0000313|Proteomes:UP000010116};
RN   [1] {ECO:0000313|EMBL:EJP73512.1, ECO:0000313|Proteomes:UP000010116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA   Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA   Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA   Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT   "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT   lineage.";
RL   ISME J. 6:1186-1199(2012).
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|ARBA:ARBA00011233, ECO:0000256|HAMAP-
CC       Rule:MF_00107}.
CC   -!- SIMILARITY: Belongs to the IspF family. {ECO:0000256|ARBA:ARBA00008480,
CC       ECO:0000256|HAMAP-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH611165; EJP73512.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4V4T3; -.
DR   HOGENOM; CLU_042800_2_6_6; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000010116; Unassembled WGS sequence.
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; 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; 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:UP000010116}.
FT   DOMAIN          226..378
FT                   /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT                   synthase"
FT                   /evidence="ECO:0000259|Pfam:PF02542"
FT   BINDING         232..234
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         232
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT   BINDING         234
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT   BINDING         258..259
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         266
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT   BINDING         280..282
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         285..289
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         356..359
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            258
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
FT   SITE            357
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00107"
SQ   SEQUENCE   381 AA;  42489 MW;  54968416C8BF16C5 CRC64;
     MIKNQNKIIG IIPAAGIGER FGSKTPKQYF RLDSNTIIEK TIDIFINHQN IDTVYVAVSE
     KDHLINDQSF CKHPKIKLVI GGSSRGESVL NCLNKAAKDG ALFSIVHDAV RPNITSNDID
     QLIQHKDDYD LVFFYRPITD SIKIKDSIKD KTVKKDDYYI VQTPQIAKTK TLRDVLLSCV
     NNNIDIPDES FAMEMHDKDI HKILGRTSNI KITHKDDLDL ISKKTKYGIG YDIHSYRDGS
     GFKLGGHFIK CDFSIVAHSD GDVLIHSISD AILGALGIGD IGIFFNDNDP ENKDMDSASI
     FKFCIEKLEA MNYEILHIDA NIICQQPKIN PQRDDILNSL AGLLNLDINQ LSIKATTTER
     LGNIGANKAM AVESIVTIGK L
//
DBGET integrated database retrieval system