AC MF_02068; DC Protein; auto TR HAMAP; MF_02068; -; 1; level=0 XX Names: TarI XX ID TARI DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase; DE EC=2.7.7.40; case GN Name=tarI; end case XX CC -!- FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to D- CC ribitol 5-phosphate. CC -!- CATALYTIC ACTIVITY: CC Reaction=CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + CC diphosphate; Xref=Rhea:RHEA:12456, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57608, CC ChEBI:CHEBI:57695; EC=2.7.7.40; case CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid CC biosynthesis. end case CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI CC subfamily. XX DR PROSITE; PS01295; ISPD; 1; trigger=no DR Pfam; PF01128; IspD; 1; trigger=no XX KW Nucleotidyltransferase KW Transferase case KW Cell wall biogenesis/degradation KW Teichoic acid biosynthesis end case XX GO GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity case GO GO:1902012; P:poly(ribitol phosphate) teichoic acid biosynthetic process end case XX FT From: TARI_STRR6 (Q8DPI2) FT BINDING 7..10 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT Optional; Condition: [LF]-A-G-G FT BINDING 82..88 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT Optional; Condition: G-x(3)-[NQ]-x-[ST] FT BINDING 113 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT Optional; Condition: S FT SITE 14 FT /note="Transition state stabilizer" FT Condition: R FT SITE 22 FT /note="Transition state stabilizer" FT Condition: K FT SITE 161 FT /note="Positions ribitol 5-phosphate for the nucleophilic FT attack" FT Condition: R FT SITE 218 FT /note="Positions ribitol 5-phosphate for the nucleophilic FT attack" FT Condition: K XX Size: 220-260; Related: None; Template: Q8DPI2; Q8RKI9; Q2G1C0; Q2G2C4; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in STAA8, STAAB, STAAC, STAAM, STAAN, STAAR, STAAS, STAAW Plasmid: None Comments: None XX # Revision 1.6 2022/11/19 //