ID G9Z3E5_9ENTR Unreviewed; 216 AA.
AC G9Z3E5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_00108};
DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_00108};
DE AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE Short=MCT {ECO:0000256|HAMAP-Rule:MF_00108};
GN Name=ispD {ECO:0000256|HAMAP-Rule:MF_00108};
GN ORFNames=HMPREF0880_02051 {ECO:0000313|EMBL:EHM49030.1};
OS Yokenella regensburgei ATCC 43003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Yokenella.
OX NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM49030.1, ECO:0000313|Proteomes:UP000003044};
RN [1] {ECO:0000313|EMBL:EHM49030.1, ECO:0000313|Proteomes:UP000003044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM49030.1,
RC ECO:0000313|Proteomes:UP000003044};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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, ECO:0000256|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:0000256|ARBA:ARBA00001282, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004787, ECO:0000256|HAMAP-
CC Rule:MF_00108}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00108}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789, ECO:0000256|HAMAP-
CC Rule:MF_00108}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00108}.
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:EHM49030.1}.
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DR EMBL; AGCL01000030; EHM49030.1; -; Genomic_DNA.
DR AlphaFoldDB; G9Z3E5; -.
DR STRING; 1002368.HMPREF0880_02051; -.
DR PATRIC; fig|1002368.3.peg.1882; -.
DR HOGENOM; CLU_061281_3_1_6; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000003044; Unassembled WGS sequence.
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 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 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, ECO:0000256|HAMAP-
KW Rule:MF_00108};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00108};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00108}.
FT SITE 7
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 137
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT SITE 193
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ SEQUENCE 216 AA; 23553 MW; 96F6B2764611B36E CRC64;
MQTECPKQYL SIGNKTILEH AVAALLAHPR VQRVVIAVSA GDARFQALPL SLHPQVTVVE
GGNERADSVL AGLKAAGDAE WVLVHDAARP CLHQDDLERL LKLSETSRVG GILAAPVRDT
MKRGEPGKAA IAHTVDRNDL WHALTPQFFP RELLIDCLTR ALDEGATITD EASALEYCGF
HPELVAGRAD NIKVTRPEDL ALAEFYLTRS EHQETA
//
