ID PURL_SACI2 Reviewed; 709 AA. AC C3MQF3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 10-JUN-2026, entry version 78. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420}; GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00420}; GN OrderedLocusNames=LS215_1611; OS Saccharolobus islandicus (strain L.S.2.15 / Lassen #1) (Sulfolobus OS islandicus). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=429572; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L.S.2.15 / Lassen #1; RX PubMed=19435847; DOI=10.1073/pnas.0808945106; RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.; RT "Biogeography of the Sulfolobus islandicus pan-genome."; RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009). CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes the CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and CC glutamate. The FGAM synthase complex is composed of three subunits. CC PurQ produces an ammonia molecule by converting glutamine to glutamate. CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- CC dependent manner. PurS interacts with PurQ and PurL and is thought to CC assist in the transfer of the ammonia molecule from PurQ to PurL. CC {ECO:0000255|HAMAP-Rule:MF_00420}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L- CC glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D- CC ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+); CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287, CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00420}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 PurL, CC 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00420}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}. CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001399; ACP35616.1; -; Genomic_DNA. DR RefSeq; WP_012713791.1; NC_012589.1. DR AlphaFoldDB; C3MQF3; -. DR SMR; C3MQF3; -. DR GeneID; 7807991; -. DR GeneID; 7810114; -. DR KEGG; sis:LS215_1611; -. DR HOGENOM; CLU_003100_0_1_2; -. DR OrthoDB; 8251at2157; -. DR UniPathway; UPA00074; UER00128. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02203; PurL_repeat1; 1. DR CDD; cd02204; PurL_repeat2; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2. DR HAMAP; MF_00420; PurL_2; 1. DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL. DR InterPro; IPR041609; PurL_linker. DR InterPro; IPR010918; PurM-like_C_dom. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR NCBIfam; TIGR01736; FGAM_synth_II; 1. DR NCBIfam; NF002290; PRK01213.1; 1. DR PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1. DR PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1. DR Pfam; PF00586; AIRS; 2. DR Pfam; PF02769; AIRS_C; 2. DR Pfam; PF18072; FGAR-AT_linker; 1. DR PIRSF; PIRSF001587; FGAM_synthase_II; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Purine biosynthesis. FT CHAIN 1..709 FT /note="Phosphoribosylformylglycinamidine synthase subunit FT PurL" FT /id="PRO_1000206046" FT ACT_SITE 36 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT ACT_SITE 84 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 80 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 82 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 83..86 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 105 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 106 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 226 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 252 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 294..296 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 470 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 507 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 510 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" SQ SEQUENCE 709 AA; 77165 MW; 9C41095D1EB3F232 CRC64; MGLNLLPIEM DDIRKRLDRE PNEIEWRVID AVWSEHCSYK SSKIFLKSFS IDSPNVIMGI KDWQDAGAVD IGDGWAIVIK VESHNHPSAI DPFNGAATGV GGIIRDIISK GAKPIALMDM IRVGNLKIRK NVWLLKNIIA GIAAYGNSIG VPVVGGELSF DDTYNDNPLV DVAAIGIVRK DKIKPSIVDK AGLKLVLAGL TGIDGLGGAS FASRKLSGED EIGAVQIADP FAGKIILDVT LEIADKVEAI KDLGGGGLAV AVTEMANGLG AIVDIEKIPL RVKNMDPADV IISETQERML YAVEEKNVEE VCKAFEEYEY PCSVIGEITS EPIIKFRYFG KDLVSLPTNA LLEPPKFLWP IKNVRKNVEE KNVDLSLEST IYTVLSHPDL VSKEWVYSQF DYEVNTSTVV KPGDANGAVV SLPNGKLLAI KADGNPDLCS EDAYECGKGI VAEAYRNLAT VGARGMVAVD HLQFGDPKKP EVYYTFVEAI RGIGEATRFF NIPIVGGKVS FYNENSQGKP IKPTPLIVMA GLVQGKLLKN RVEDSSYVVL LGYTRKELGG SLLSKIFKVP SQAPKVRLQE DLLSSEVVID AINEEKITFA KDISRGGLAA SLFNIIVHGY GVEISTKSIL SDTDNVVENL FSESSGRFVI LTNEPEWIVE KSRSKGIVAS IIGKVNKKTS ILTIDNTDYD LKTIVNNYFN FLEEVIGNG //