SMART: Pfam domain IspD

The domain within your query sequence starts at position 45 and ends at position 277; the E-value for the IspD domain shown below is 2.5e-40.

VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMR
SIIQRYGHKRISLAEAGATRHRSIFNGLKALAEDQPDCKLTKPEVVIIHDAVRPFVEEDI
LLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKHRASEMPQAFLFDVIYEAY
QQCSDFDLEFGTECLQLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMIKE

IspD

PFAM accession number:	PF01128
Interpro abstract (IPR034683):	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) catalyses the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) in the deoxyxylulose pathway of isopentenyl diphosphate (IPP) biosynthesis [ (PUBMED:10841550) ]. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. The isoprenoid pathway is a well known target for anti-infective drug development [ (PUBMED:17081012) (PUBMED:17921290) ]. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. Ribitol-5-phosphate cytidylyltransferase (TarI) is required for the synthesis of activated ribitol via the wall teichoic acid biosynthesis pathway. The enzyme catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate to form CDP-ribitol [ (PUBMED:19074383) ]. The human IspD (known as D-ribitol-5-phosphate cytidylyltransferase or isoprenoid synthase domain-containing protein) shows a canonical N-terminal cytidyltransferase domain linked to a C-terminal domain that is absent in cytidyltransferase homologues. It has cytidyltransferase activity toward pentose phosphates, including ribulose 5-phosphate, ribose 5-phosphate, and ribitol 5-phosphate. It has benn implicated in dystroglycan O-mannosylation [ (PUBMED:26687144) (PUBMED:27194101) ]. This family consists of cytidylyltransferases IspD and TarI.
GO function:	cytidylyltransferase activity (GO:0070567)

PFAM accession number:

PF01128

Interpro abstract (IPR034683):

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) catalyses the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) in the deoxyxylulose pathway of isopentenyl diphosphate (IPP) biosynthesis [ (PUBMED:10841550) ]. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. The isoprenoid pathway is a well known target for anti-infective drug development [ (PUBMED:17081012) (PUBMED:17921290) ]. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein.

Ribitol-5-phosphate cytidylyltransferase (TarI) is required for the synthesis of activated ribitol via the wall teichoic acid biosynthesis pathway. The enzyme catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate to form CDP-ribitol [ (PUBMED:19074383) ].

The human IspD (known as D-ribitol-5-phosphate cytidylyltransferase or isoprenoid synthase domain-containing protein) shows a canonical N-terminal cytidyltransferase domain linked to a C-terminal domain that is absent in cytidyltransferase homologues. It has cytidyltransferase activity toward pentose phosphates, including ribulose 5-phosphate, ribose 5-phosphate, and ribitol 5-phosphate. It has benn implicated in dystroglycan O-mannosylation [ (PUBMED:26687144) (PUBMED:27194101) ].

This family consists of cytidylyltransferases IspD and TarI.

GO function:

cytidylyltransferase activity (GO:0070567)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry IspD