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 03-AUG-2022, entry version 141.
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; DOI=10.1016/s0021-9258(17)37310-6;
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}.
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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 AlphaFoldDB; Q06755; -.
DR SMR; Q06755; -.
DR STRING; 224308.BSU00900; -.
DR PaxDb; Q06755; -.
DR PRIDE; Q06755; -.
DR EnsemblBacteria; CAB11866; CAB11866; BSU_00900.
DR GeneID; 936855; -.
DR KEGG; bsu:BSU00900; -.
DR PATRIC; fig|224308.179.peg.91; -.
DR eggNOG; COG1211; Bacteria.
DR InParanoid; Q06755; -.
DR OMA; ERQHSVY; -.
DR PhylomeDB; Q06755; -.
DR BioCyc; BSUB:BSU00900-MON; -.
DR BRENDA; 2.7.7.60; 658.
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;
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:0007829|PDB:5DDT"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 155..165
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:5DDT"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5DDT"
FT HELIX 213..226
FT /evidence="ECO:0007829|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
