ID A3CQX4_STRSV Unreviewed; 240 AA.
AC A3CQX4;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Ribitol-5-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_02068};
DE EC=2.7.7.40 {ECO:0000256|HAMAP-Rule:MF_02068};
GN Name=tarI {ECO:0000256|HAMAP-Rule:MF_02068};
GN OrderedLocusNames=SSA_2214 {ECO:0000313|EMBL:ABN45579.1};
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919 {ECO:0000313|EMBL:ABN45579.1, ECO:0000313|Proteomes:UP000002148};
RN [1] {ECO:0000313|EMBL:ABN45579.1, ECO:0000313|Proteomes:UP000002148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36 {ECO:0000313|EMBL:ABN45579.1,
RC ECO:0000313|Proteomes:UP000002148};
RX PubMed=17277061; DOI=10.1128/JB.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
CC -!- FUNCTION: Catalyzes the transfer of the cytidylyl group of CTP to D-
CC ribitol 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_02068}.
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 -!- 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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02068};
CC -!- PATHWAY: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02068}.
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 -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. TarI
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02068}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02068}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000387; ABN45579.1; -; Genomic_DNA.
DR RefSeq; WP_002899243.1; NC_009009.1.
DR RefSeq; YP_001036129.1; NC_009009.1.
DR AlphaFoldDB; A3CQX4; -.
DR STRING; 388919.SSA_2214; -.
DR KEGG; ssa:SSA_2214; -.
DR PATRIC; fig|388919.9.peg.2099; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_3_9; -.
DR OrthoDB; 9806837at2; -.
DR UniPathway; UPA00056; UER00093.
DR UniPathway; UPA00790; -.
DR Proteomes; UP000002148; Chromosome.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047349; F:D-ribitol-5-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:1902012; P:poly(ribitol phosphate) teichoic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR HAMAP; MF_02068; TarI; 1.
DR InterPro; IPR001228; IspD.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR018294; ISPD_synthase_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR034709; TarI.
DR NCBIfam; TIGR00453; ispD; 1.
DR PANTHER; PTHR43015; D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE; 1.
DR PANTHER; PTHR43015:SF1; D-RIBITOL-5-PHOSPHATE CYTIDYLYLTRANSFERASE; 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 Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02068};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_02068}; Reference proteome {ECO:0000313|Proteomes:UP000002148};
KW Teichoic acid biosynthesis {ECO:0000256|ARBA:ARBA00022944,
KW ECO:0000256|HAMAP-Rule:MF_02068};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02068}.
FT BINDING 8..11
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT BINDING 81..87
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 15
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 23
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 159
FT /note="Positions ribitol 5-phosphate for the nucleophilic
FT attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
FT SITE 216
FT /note="Positions ribitol 5-phosphate for the nucleophilic
FT attack"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02068"
SQ SEQUENCE 240 AA; 26508 MW; F88A93F7E0AA1803 CRC64;
MTTSALIFAG GTGSRMNTKT LPKQFLELHG KPIIIHTIEH FEDHPAVSDI VVVCVDGWLD
YCRDLLARFN IKKVSQVVPG GKTGQMSIFN GLSVLREKYK NDDDYVLIHD GVRPLIDGGI
ISKNIEAAKK YGAAITVKPV IETVIQVDEA DVINQVIERS TCQTAVAPQT FALSKIHSLH
LKAQAENQFD MTDSATLARY FGLPLHTVMG GSENIKITTP SDFYIFRAIY EARENAQIFG
//