UniProt functional annotation for P49058



	UniProt functional annotation for P49058

UniProt code: P49058.

Organism: Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680).

Taxonomy: Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.

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. Essential for mouse infection by tick bite and critical for the survival in environments that appear to lack sufficient amounts of guanine, guanosine, and/or deoxyguanosine to support spirochete growth, such as mammalian host tissues. {ECO:0000269|PubMed:19666713, ECO:0000269|PubMed:9268334}.

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:0000269|PubMed:9268334};

Cofactor: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:9268334};

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:0000250|UniProtKB:P0ADG7}.

Biophysicochemical properties: Kinetic parameters: KM=29 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:9268334}; KM=1100 uM for NAD(+) {ECO:0000269|PubMed:9268334};

Pathway: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000305|PubMed:9268334}.

Subunit: Homotetramer. {ECO:0000269|PubMed:9268334}.

Similarity: Belongs to the IMPDH/GMPR family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680).
Taxonomy:		Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.



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. Essential for mouse infection by tick bite and critical for the survival in environments that appear to lack sufficient amounts of guanine, guanosine, and/or deoxyguanosine to support spirochete growth, such as mammalian host tissues. {ECO:0000269\|PubMed:19666713, ECO:0000269\|PubMed:9268334}.


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:0000269\|PubMed:9268334};
Cofactor:		Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000269\|PubMed:9268334};
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:0000250\|UniProtKB:P0ADG7}.
Biophysicochemical properties:		Kinetic parameters: KM=29 uM for Inosine 5'-phosphate {ECO:0000269\|PubMed:9268334}; KM=1100 uM for NAD(+) {ECO:0000269\|PubMed:9268334};
Pathway:		Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000305\|PubMed:9268334}.
Subunit:		Homotetramer. {ECO:0000269\|PubMed:9268334}.
Similarity:		Belongs to the IMPDH/GMPR family. {ECO:0000305}.