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Database: UniProt
Entry: A0A1U7NEF2_9FIRM
LinkDB: A0A1U7NEF2_9FIRM
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ID   A0A1U7NEF2_9FIRM        Unreviewed;       221 AA.
AC   A0A1U7NEF2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|ARBA:ARBA00019056};
DE            EC=2.7.7.60 {ECO:0000256|ARBA:ARBA00012526};
GN   ORFNames=BO222_09325 {ECO:0000313|EMBL:OLU37904.1};
OS   Ileibacterium valens.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Ileibacterium.
OX   NCBI_TaxID=1862668 {ECO:0000313|EMBL:OLU37904.1, ECO:0000313|Proteomes:UP000186341};
RN   [1] {ECO:0000313|EMBL:OLU37904.1, ECO:0000313|Proteomes:UP000186341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NYU-BL-A3 {ECO:0000313|EMBL:OLU37904.1,
RC   ECO:0000313|Proteomes:UP000186341};
RA   Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA   Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT   "Description of two novel members of the family Erysipelotrichaceae:
RT   Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT   gen. nov., sp. nov.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002459}.
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:0000256|ARBA:ARBA00001282};
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:0000256|ARBA:ARBA00004787}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000256|ARBA:ARBA00009789}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLU37904.1}.
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DR   EMBL; MPJW01000186; OLU37904.1; -; Genomic_DNA.
DR   RefSeq; WP_075820476.1; NZ_MPJW01000186.1.
DR   AlphaFoldDB; A0A1U7NEF2; -.
DR   GeneID; 82203363; -.
DR   OrthoDB; 9806837at2; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000186341; Unassembled WGS sequence.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR00453; ispD; 1.
DR   PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:OLU37904.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186341};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OLU37904.1}.
SQ   SEQUENCE   221 AA;  24802 MW;  DD32B63A6A2AAEA5 CRC64;
     MPAYSAIILA AGKGSRTHLD YNKVFYHLDS NHTVLDRSLE LFESDPDCKQ IIGVCASYEK
     DYVEKNYSKY SKLSWTVGGN TRQESVFNGL QKVKMPVVMI HDGARPFLKR ESLEALKHMM
     NFEKAALLMT PAIDTIKIVD ESGYVVMTPA REQIYHAQTP QAFMTDLILQ AHLEAQKTGI
     EGTDDAQLVE RFTHVPVACV IGDPSNTKIT NPDDLDHLVQ D
//
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