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UniProt functional annotation for P0C0H6 | ||
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| UniProt code: P0C0H6. |
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| Organism: | |
Streptococcus pyogenes. |
| Taxonomy: | |
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus. |
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| Function: | |
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. {ECO:0000255|HAMAP-Rule:MF_01964}. |
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| Catalytic activity: | |
Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; |
| Cofactor: | |
Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; |
| Activity regulation: | |
Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH. {ECO:0000255|HAMAP-Rule:MF_01964}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=62 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:10200156}; KM=1180 uM for NAD(+) {ECO:0000269|PubMed:10200156}; pH dependence: Optimum pH is 7.8. {ECO:0000269|PubMed:10200156}; |
| Pathway: | |
Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}. |
| Subunit: | |
Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:10200156}. |
| Mass spectrometry: | |
Mass=52328; Method=MALDI; Evidence={ECO:0000269|PubMed:10200156}; |
| Similarity: | |
Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP- Rule:MF_01964}. |
Annotations taken from UniProtKB at the EBI.