(data stored in SCRATCH zone)

SWISSPROT: C8W3W0_DESAS

ID   C8W3W0_DESAS            Unreviewed;       232 AA.
AC   C8W3W0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000256|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000256|HAMAP-Rule:MF_00108};
GN   OrderedLocusNames=Dtox_0261 {ECO:0000313|EMBL:ACV61214.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61214.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61214.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-
CC       methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-
CC       phosphate (MEP). {ECO:0000256|HAMAP-Rule:MF_00108,
CC       ECO:0000256|SAAS:SAAS00786778}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-
CC         2-C-methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00108,
CC         ECO:0000256|SAAS:SAAS01130198};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00108, ECO:0000256|SAAS:SAAS01130190}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family.
CC       IspD subfamily. {ECO:0000256|HAMAP-Rule:MF_00108,
CC       ECO:0000256|SAAS:SAAS00888088}.
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; CP001720; ACV61214.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0261; -.
DR   EnsemblBacteria; ACV61214; ACV61214; Dtox_0261.
DR   KEGG; dae:Dtox_0261; -.
DR   eggNOG; ENOG4105CE5; Bacteria.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000218563; -.
DR   KO; K00991; -.
DR   OMA; ERQHSVY; -.
DR   BioCyc; DACE485916:G1GFV-271-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
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   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00453; ispD; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W3W0.
DR   SWISS-2DPAGE; C8W3W0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS01130196};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS00981526, ECO:0000313|EMBL:ACV61214.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00108,
KW   ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:ACV61214.1}.
FT   SITE         16     16       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00108}.
FT   SITE         23     23       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00108}.
FT   SITE        156    156       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
FT   SITE        212    212       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_00108}.
SQ   SEQUENCE   232 AA;  25395 MW;  1AA6289B8BBD358E CRC64;
     MSLISTIITA AGQGLRMGTD TRKQYLSLQG KPILSYAIET FIGMPAVNNI ILVVSPGDES
     FCLENIIPIH GRSKVQAVVA GGASRQESVY NGLLALPQGT NLVIIHDGVR PLFEGNEIDA
     LLEAAAVNGA ATLAVPPKDT VKLVNEYNKV VRTLPRERLW LTQTPQVFKY DIIMNAHQKA
     RRHGFEATDD ASLVEVSGQQ VRVIEGSYEN IKITTPEDMI IAEAILNRRK HK
//

If you have problems or comments...

PBIL Back to PBIL home page