UniProt functional annotation for Q756Z6

UniProt code: Q756Z6.

Organism:		Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
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:0000256|HAMAP-Rule:MF_03156}.
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:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928};
Cofactor:		Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-Rule:MF_03156};
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:0000256|HAMAP-Rule:MF_03156}.
Pathway:		Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}.
Subunit:		Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03156}.
Subcellular location:		Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}.
Similarity:		Belongs to the IMPDH/GMPR family. {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003927}.

Annotations taken from UniProtKB at the EBI.