(data stored in ACNUC7421 zone)

SWISSPROT: ISPD_BACSU

ID   ISPD_BACSU              Reviewed;         232 AA.
AC   Q06755;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   11-DEC-2019, entry version 132.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
DE            EC=2.7.7.60;
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase;
DE   AltName: Full=MEP cytidylyltransferase;
DE            Short=MCT;
GN   Name=ispD; Synonyms=yacM; OrderedLocusNames=BSU00900;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7510287;
RA   Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M.,
RA   Lapointe J.;
RT   "Clustering and co-transcription of the Bacillus subtilis genes encoding
RT   the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and
RT   the first enzyme for cysteine biosynthesis.";
RL   J. Biol. Chem. 269:7473-7482(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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:0000250}.
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   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 2/6.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000305}.
DR   EMBL; L14580; AAA21794.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05324.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11866.1; -; Genomic_DNA.
DR   PIR; S66119; S66119.
DR   RefSeq; NP_387971.1; NC_000964.3.
DR   RefSeq; WP_003235019.1; NZ_JNCM01000029.1.
DR   PDB; 5DDT; X-ray; 1.80 A; A/B=1-232.
DR   PDB; 5DDV; X-ray; 2.30 A; A=1-232.
DR   PDB; 5HS2; X-ray; 1.90 A; A/B=1-232.
DR   PDBsum; 5DDT; -.
DR   PDBsum; 5DDV; -.
DR   PDBsum; 5HS2; -.
DR   SMR; Q06755; -.
DR   STRING; 224308.BSU00900; -.
DR   PaxDb; Q06755; -.
DR   PRIDE; Q06755; -.
DR   EnsemblBacteria; CAB11866; CAB11866; BSU00900.
DR   GeneID; 936855; -.
DR   KEGG; bsu:BSU00900; -.
DR   PATRIC; fig|224308.179.peg.91; -.
DR   eggNOG; ENOG4105CE5; Bacteria.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000218563; -.
DR   InParanoid; Q06755; -.
DR   KO; K00991; -.
DR   OMA; ERQHSVY; -.
DR   PhylomeDB; Q06755; -.
DR   BioCyc; BSUB:BSU00900-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IBA:GO_Central.
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   1: Evidence at protein level;
DR   PRODOM; Q06755.
DR   SWISS-2DPAGE; Q06755.
KW   3D-structure; Isoprene biosynthesis; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..232
FT                   /note="2-C-methyl-D-erythritol 4-phosphate
FT                   cytidylyltransferase"
FT                   /id="PRO_0000075551"
FT   SITE            15
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            22
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            152
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000250"
FT   SITE            209
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        57
FT                   /note="E -> D (in Ref. 1; AAA21794)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..9
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          12..14
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           22..24
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           32..42
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          46..53
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           55..57
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           58..67
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          71..78
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           83..92
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          96..102
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           112..125
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          126..133
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          138..142
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          145..149
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          155..165
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           166..179
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           186..192
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   STRAND          199..202
FT                   /evidence="ECO:0000244|PDB:5DDT"
FT   HELIX           213..226
FT                   /evidence="ECO:0000244|PDB:5DDT"
SQ   SEQUENCE   232 AA;  25843 MW;  FFCDDDB266F2A3DB CRC64;
     MSYDVVIPAA GQGKRMKAGR NKLFIELKGD PVIIHTLRVF DSHRQCDKII LVINEQEREH
     FQQLLSDYPF QTSIELVAGG DERQHSVYKG LKAVKQEKIV LVHDGARPFI KHEQIDELIA
     EAEQTGAAIL AVPVKDTIKR VQDLQVSETI ERSSLWAVQT PQAFRLSLLM KAHAEAERKG
     FLGTDDASLV EQMEGGSVRV VEGSYTNIKL TTPDDLTSAE AIMESESGNK HV
//

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