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HAMAP rule MF_00420

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_00420
Accession MF_00420
Dates 26-JUN-2001 (Created)
3-SEP-2024 (Last updated, Version 48)
Name PurL_2
Scope(s) Bacteria
Archaea
Template(s) P12042 (PURL_BACSU); Q9X0X3 (PURL_THEMA); Q5SMH8 (PURL_THET8); [ Recover all ]
Triggered by HAMAP; MF_00420 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PURL
Protein name RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL;
                 Short=FGAM synthase;
                 EC=6.3.5.3;
AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II;
                 Short=FGAR amidotransferase II;
                 Short=FGAR-AT II;
AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II;
AltName: Full=Glutamine amidotransferase PurL;
Gene name Name=purL;

Comments [?]

FUNCTIONPart 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.
CATALYTIC ACTIVITY Reaction=N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L- glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D- ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+); 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;
PATHWAYPurine 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.
SUBUNITMonomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the FGAMS family.

Keywords [?]

ATP-binding
Cytoplasm
Ligase
Metal-binding
Magnesium
Nucleotide-binding
Purine biosynthesis

Gene Ontology [?]

GO:0000287; Molecular function:magnesium ion binding
GO:0005524; Molecular function:ATP binding
GO:0004642; Molecular function:phosphoribosylformylglycinamidine synthase activity
GO:0006189; Biological process:'de novo' IMP biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF00586; AIRS; 1;
Pfam PF02769; AIRS_C; 1;
NCBIfam TIGR01736; FGAM_synth_II; 1;

Features [?]

From: PURL_THEMA (Q9X0X3)
Key From To Description Tag Condition FTGroup
BINDING 71 74 /ligand="substrate" S-H-N-H
BINDING 280 282 /ligand="substrate" E-S-Q
ACT_SITE 32 32 H
ACT_SITE 72 72 /note="Proton acceptor" H
BINDING 70 70 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"		 E
BINDING 94 94 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"		 D
BINDING 236 236 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"		 D
BINDING 478 478 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"		 N
BINDING 35 35 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 Y
BINDING 68 68 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [KR]
BINDING 93 93 /ligand="substrate" R
BINDING 189 189 /ligand="substrate" R
BINDING 208 208 /ligand="substrate" Q
BINDING 442 442 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [ND]
BINDING 477 477 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
BINDING 480 480 /ligand="substrate" S

Additional information [?]

Size range 603-824 amino acids
Related rules MF_00419
Fusion Nter: None Cter: None
Comments FGAM synthase can be composed of a single polypeptide (large PurL, MF_00419), or it can be composed of three separate proteins: PurL (small PurL, MF_00420), PurQ (MF_00421) and PurS (MF_01926).



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