Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,256 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-serine Identifier CHEBI:33384 Charge 0 Formula C3H7NO3 InChIKeyhelp_outline MTCFGRXMJLQNBG-REOHCLBHSA-N SMILEShelp_outline [NH3+][C@@H](CO)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 76 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 835 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O-phospho-L-serine Identifier CHEBI:57524 Charge -2 Formula C3H6NO6P InChIKeyhelp_outline BZQFBWGGLXLEPQ-REOHCLBHSA-L SMILEShelp_outline [NH3+][C@@H](COP([O-])([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:59112 | RHEA:59113 | RHEA:59114 | RHEA:59115 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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SbnI is a free serine kinase that generates O-phospho-L-serine for staphyloferrin B biosynthesis in Staphylococcus aureus.
Verstraete M.M., Perez-Borrajero C., Brown K.L., Heinrichs D.E., Murphy M.E.P.
Staphyloferrin B (SB) is an iron-chelating siderophore produced by <i>Staphylococcus aureus</i> in invasive infections. Proteins for SB biosynthesis and export are encoded by the <i>sbnABCDEFGHI</i> gene cluster, in which SbnI, a member of the ParB/Srx superfamily, acts as a heme-dependent transcr ... >> More
Staphyloferrin B (SB) is an iron-chelating siderophore produced by <i>Staphylococcus aureus</i> in invasive infections. Proteins for SB biosynthesis and export are encoded by the <i>sbnABCDEFGHI</i> gene cluster, in which SbnI, a member of the ParB/Srx superfamily, acts as a heme-dependent transcriptional regulator of the <i>sbn</i> locus. However, no structural or functional information about SbnI is available. Here, a crystal structure of SbnI revealed striking structural similarity to an ADP-dependent free serine kinase, SerK, from the archaea <i>Thermococcus kodakarensis</i> We found that features of the active sites are conserved, and biochemical assays and <sup>31</sup>P NMR and HPLC analyses indicated that SbnI is also a free serine kinase but uses ATP rather than ADP as phosphate donor to generate the SB precursor <i>O</i>-phospho-l-serine (OPS). SbnI consists of two domains, and elevated <i>B</i>-factors in domain II were consistent with the open-close reaction mechanism previously reported for SerK. Mutagenesis of Glu<sup>20</sup> and Asp<sup>58</sup> in SbnI disclosed that they are required for kinase activity. The only known OPS source in bacteria is through the phosphoserine aminotransferase activity of SerC within the serine biosynthesis pathway, and we demonstrate that an <i>S. aureus serC</i> mutant is a serine auxotroph, consistent with a function in l-serine biosynthesis. However, the <i>serC</i> mutant strain could produce SB when provided l-serine, suggesting that SbnI produces OPS for SB biosynthesis <i>in vivo</i> These findings indicate that besides transcriptionally regulating the <i>sbn</i> locus, SbnI also has an enzymatic role in the SB biosynthetic pathway. << Less