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4JIS

Crystal structure of ribitol 5-phosphate cytidylyltransferase (TarI) from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008299biological_processisoprenoid biosynthetic process
A0016779molecular_functionnucleotidyltransferase activity
A0019350biological_processteichoic acid biosynthetic process
A0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
A0070567molecular_functioncytidylyltransferase activity
A0071555biological_processcell wall organization
A1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
B0003824molecular_functioncatalytic activity
B0008299biological_processisoprenoid biosynthetic process
B0016779molecular_functionnucleotidyltransferase activity
B0019350biological_processteichoic acid biosynthetic process
B0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
B0070567molecular_functioncytidylyltransferase activity
B0071555biological_processcell wall organization
B1902012biological_processpoly(ribitol phosphate) teichoic acid biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS01295
Number of Residues8
DetailsISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. IITHDSVR
ChainResidueDetails
AILE107-ARG114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02068
ChainResidueDetails
ALEU7
AGLY81
ASER112
BLEU7
BGLY81
BSER112

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_02068
ChainResidueDetails
AARG14
ALYS22
BARG14
BLYS22

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Positions ribitol 5-phosphate for the nucleophilic attack => ECO:0000255|HAMAP-Rule:MF_02068
ChainResidueDetails
AARG160
ALYS217
BARG160
BLYS217

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PDB entries from 2024-07-24

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