ID PURL_BACC0 Reviewed; 739 AA. AC B7JM85; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 02-SEP-2026, entry version 84. 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=BCAH820_0326; OS Bacillus cereus (strain AH820). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=405535; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AH820; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus AH820."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. 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; CP001283; ACK87275.1; -; Genomic_DNA. DR RefSeq; WP_000055577.1; NC_011773.1. DR AlphaFoldDB; B7JM85; -. DR SMR; B7JM85; -. DR GeneID; 45020353; -. DR KEGG; bcu:BCAH820_0326; -. DR HOGENOM; CLU_003100_0_1_9; -. 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 FunFam; 3.30.1330.10:FF:000004; Phosphoribosylformylglycinamidine synthase subunit PurL; 1. DR FunFam; 3.30.1330.10:FF:000011; Phosphoribosylformylglycinamidine synthase subunit PurL; 1. DR FunFam; 3.90.650.10:FF:000009; Phosphoribosylformylglycinamidine synthase subunit PurL; 1. DR FunFam; 3.90.650.10:FF:000013; Phosphoribosylformylglycinamidine synthase subunit PurL; 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..739 FT /note="Phosphoribosylformylglycinamidine synthase subunit FT PurL" FT /id="PRO_1000194819" FT ACT_SITE 54 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT ACT_SITE 100 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 99..102 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 121 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 122 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 273 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 317..319 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 500 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 537 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 538 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" FT BINDING 540 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420" SQ SEQUENCE 739 AA; 80175 MW; 8BEB258F69943EFF CRC64; MSLMLEPNPT QIKEERIYAE MGLTDEEFAM VEKILGRLPN YTETGLFSVM WSEHCSYKNS KPVLRKFPTT GERVLQGPGE GAGIVDIGDN QAVVFKMESH NHPSAIEPYQ GAATGVGGII RDVFSMGARP VALLNSLRFG ELQSPRVKYL FEEVVAGIAG YGNCIGIPTV GGEVQFDPCY EGNPLVNAMC VGLINHEDIK KGQAHGAGNT VMYVGASTGR DGIHGATFAS EELSESSEAK RPAVQVGDPF MEKLLIEACL ELIQSDALVG IQDMGAAGLT SSSAEMASKA GMGIEMYLDD VPQRETGMTP YEMMLSESQE RMLIVVKKGR EQEIVDLFEK YGLAAVTMGK VTEDKMLRLF HKGEMVAEVP ADALAEEAPI YHKPSKEAAY FAEFQQMKME TPKVENYKET LFALLQQPTI ASKEWVYDQY DYQVRTSTVV TPGSDAAVVR VRGTEKGLAM TTDCNSRYIY LDPEVGGKIA VAEAARNIVC SGGEPLAITD CLNFGNPEKP EIFWQIEKSV DGMSEACRTL QTPVIGGNVS MYNERSGEAV YPTPTVGMVG LVHDLKHVTT QEFKQAGDLV YVIGETKAEF GGSELQKMLH GKIFGQSPSI DLDVELKRQK QVLAAIQAGL VQSAHDVAEG GLAVAISESA IGANGLGATV KLDGEATAAL FAESQSRFVI TVKRENKEAF EKAVEAIQVG EVTNTNEVTI HNEENEVLLT ANVDEMRKAW KGAIPCLLK //