ISPD_LEPIC
ID ISPD_LEPIC Reviewed; 238 AA.
AC Q72P59;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108};
DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108};
DE AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108};
GN Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108}; OrderedLocusNames=LIC_12617;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
CC -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-
CC erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
CC {ECO:0000255|HAMAP-Rule:MF_00108}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-
CC 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:0000255|HAMAP-Rule:MF_00108};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00108}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00108}.
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DR EMBL; AE016823; AAS71177.1; -; Genomic_DNA.
DR RefSeq; WP_000838282.1; NC_005823.1.
DR AlphaFoldDB; Q72P59; -.
DR SMR; Q72P59; -.
DR PaxDb; Q72P59; -.
DR EnsemblBacteria; AAS71177; AAS71177; LIC_12617.
DR GeneID; 61142493; -.
DR KEGG; lic:LIC_12617; -.
DR HOGENOM; CLU_061281_2_2_12; -.
DR OMA; ERQHSVY; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000007037; Chromosome I.
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 PROSITE; PS01295; ISPD; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis; Nucleotidyltransferase; Transferase.
FT CHAIN 1..238
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000075581"
FT SITE 22
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 29
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 160
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 214
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
SQ SEQUENCE 238 AA; 26663 MW; C02400F042434DFB CRC64;
MKSLFLSEKI YVLILAGGTG SRMGSKIPKQ FLELNGEPIL IHSLKRFQNW GKQKRIVLVS
HFESIPKIES ICASYLENED RIVQGGENRH SSMLCGLSVL DFKDEDIILV HDAARPFVLA
DELDSLCEKV RSDGIATLAS RTSETVLEEL NGKTVSFLDR EHVWFMKTPQ GIRGDVLKEL
LTFSVDSIPT DLCSWALTFG KTSSIVESNP LNLKITRKED LDLAEVFSSL FQKISSDI
