UniProt functional annotation for Q9X0X3



	UniProt functional annotation for Q9X0X3

UniProt code: Q9X0X3.

Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8).

Taxonomy: Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.

Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481}.

Catalytic activity: Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D- ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D- ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP- Rule:MF_00420, ECO:0000269|PubMed:17154526};

Biophysicochemical properties: Kinetic parameters: KM=0.26 mM for ATP (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:17154526}; KM=1.05 mM for FGAR (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:17154526}; KM=158 mM for NH(4)Cl (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:17154526}; Note=Kcat is 0.39 sec(-1) for FGAM synthase activity with NH(4)Cl as substrate (at pH 8 and 37 degrees Celsius). Kcat is 0.40 sec(-1) for FGAM synthase activity with FGAR as substrate (at pH 8 and 37 degrees Celsius). Kcat is 0.41 sec(-1) for FGAM synthase activity with ATP as substrate (at pH 8 and 37 degrees Celsius).;

Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5- amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- Rule:MF_00420}.

Subunit: Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:16544324, ECO:0000269|PubMed:17154526, ECO:0000269|PubMed:18597481}.

Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.

Miscellaneous: Purl possesses an auxiliary ATP Binding region which is not catalytic, but able to bind additional ATP. The conformational changes associated with its binding could have a regulatory role in formation of the PurLSQ complex (PubMed:17154526). {ECO:0000305|PubMed:17154526}.

Similarity: Belongs to the FGAMS family. {ECO:0000255|HAMAP- Rule:MF_00420}.

Annotations taken from UniProtKB at the EBI.


Organism:		Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8).
Taxonomy:		Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.



Function:		Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. {ECO:0000255\|HAMAP-Rule:MF_00420, ECO:0000269\|PubMed:17154526, ECO:0000269\|PubMed:18597481}.


Catalytic activity:		Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D- ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D- ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255\|HAMAP- Rule:MF_00420, ECO:0000269\|PubMed:17154526};
Biophysicochemical properties:		Kinetic parameters: KM=0.26 mM for ATP (at pH 8 and 37 degrees Celsius) {ECO:0000269\|PubMed:17154526}; KM=1.05 mM for FGAR (at pH 8 and 37 degrees Celsius) {ECO:0000269\|PubMed:17154526}; KM=158 mM for NH(4)Cl (at pH 8 and 37 degrees Celsius) {ECO:0000269\|PubMed:17154526}; Note=Kcat is 0.39 sec(-1) for FGAM synthase activity with NH(4)Cl as substrate (at pH 8 and 37 degrees Celsius). Kcat is 0.40 sec(-1) for FGAM synthase activity with FGAR as substrate (at pH 8 and 37 degrees Celsius). Kcat is 0.41 sec(-1) for FGAM synthase activity with ATP as substrate (at pH 8 and 37 degrees Celsius).;
Pathway:		Purine metabolism; IMP biosynthesis via de novo pathway; 5- amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255\|HAMAP- Rule:MF_00420}.
Subunit:		Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits. {ECO:0000255\|HAMAP-Rule:MF_00420, ECO:0000269\|PubMed:16544324, ECO:0000269\|PubMed:17154526, ECO:0000269\|PubMed:18597481}.
Subcellular location:		Cytoplasm {ECO:0000255\|HAMAP-Rule:MF_00420}.
Miscellaneous:		Purl possesses an auxiliary ATP Binding region which is not catalytic, but able to bind additional ATP. The conformational changes associated with its binding could have a regulatory role in formation of the PurLSQ complex (PubMed:17154526). {ECO:0000305\|PubMed:17154526}.
Similarity:		Belongs to the FGAMS family. {ECO:0000255\|HAMAP- Rule:MF_00420}.