ISPD_BUCAI
ID ISPD_BUCAI Reviewed; 237 AA.
AC P57495;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
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; OrderedLocusNames=BU420;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000003; BAB13118.1; -; Genomic_DNA.
DR RefSeq; NP_240232.1; NC_002528.1.
DR RefSeq; WP_010896106.1; NC_002528.1.
DR AlphaFoldDB; P57495; -.
DR SMR; P57495; -.
DR STRING; 107806.10039084; -.
DR EnsemblBacteria; BAB13118; BAB13118; BAB13118.
DR KEGG; buc:BU420; -.
DR PATRIC; fig|107806.10.peg.429; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_3_1_6; -.
DR OMA; ERQHSVY; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000001806; 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;
KW Isoprene biosynthesis; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..237
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000075557"
FT SITE 23
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 30
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000250"
FT SITE 216
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000250"
SQ SEQUENCE 237 AA; 26922 MW; 3E8AFDEF35BCB706 CRC64;
MILVNLFEPK IIAIVPAAGI GSRMKIDVPK QYIKIQNRTI LEHTLTTLLL HPNIVQIIVS
LNKKDNYFHK LSISSNFRII SVVGGEKRIN SVLSGLIVVK NVDWVIVHDA VRPCLSYKDL
EKLISIIKKN PVGAILARPV SDTIKYSNLK QKKAVYTVYR KNLWHALTPQ LFQVELLKNC
LKKIIKDQIS VTDEASALEY CGYNPLLVLG SCRNIKITWP EDLVLANFYL KNHIIDK
