ID PUR4_PASMU Reviewed; 1297 AA. AC Q9CLW4; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-SEP-2026, entry version 150. DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419}; DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419}; GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=PM1085; OS Pasteurella multocida (strain Pm70). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Pasteurella. OX NCBI_TaxID=272843; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pm70; RX PubMed=11248100; DOI=10.1073/pnas.051634598; RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.; RT "Complete genomic sequence of Pasteurella multocida Pm70."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001). CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield CC formylglycinamidine ribonucleotide (FGAM) and glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00419}. 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_00419}; 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_00419}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}. CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family. CC {ECO:0000255|HAMAP-Rule:MF_00419}. 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; AE004439; AAK03169.1; -; Genomic_DNA. DR RefSeq; WP_010907012.1; NC_002663.1. DR AlphaFoldDB; Q9CLW4; -. DR SMR; Q9CLW4; -. DR STRING; 272843.PM1085; -. DR EnsemblBacteria; AAK03169; AAK03169; PM1085. DR KEGG; pmu:PM1085; -. DR PATRIC; fig|272843.6.peg.1099; -. DR HOGENOM; CLU_001031_0_2_6; -. DR OrthoDB; 9804441at2; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000000809; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP 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; cd01740; GATase1_FGAR_AT; 1. DR CDD; cd02203; PurL_repeat1; 1. DR CDD; cd02204; PurL_repeat2; 1. DR FunFam; 1.10.8.750:FF:000002; Phosphoribosylformylglycinamidine synthase; 1. DR FunFam; 3.30.1330.10:FF:000002; Phosphoribosylformylglycinamidine synthase; 1. DR FunFam; 3.30.1330.10:FF:000005; Phosphoribosylformylglycinamidine synthase; 1. DR FunFam; 3.40.50.880:FF:000008; Phosphoribosylformylglycinamidine synthase; 1. DR FunFam; 3.90.650.10:FF:000002; Phosphoribosylformylglycinamidine synthase; 1. DR FunFam; 3.90.650.10:FF:000005; Phosphoribosylformylglycinamidine synthase; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 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_00419; PurL_1; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR040707; FGAR-AT_N. DR InterPro; IPR055181; FGAR-AT_PurM_N-like. DR InterPro; IPR010073; PurL_large. DR InterPro; IPR041609; PurL_linker. DR InterPro; IPR010918; PurM-like_C_dom. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR036604; PurS-like_sf. DR NCBIfam; TIGR01735; FGAM_synt; 1. DR NCBIfam; NF003672; PRK05297.1; 1. DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1. DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1. DR Pfam; PF02769; AIRS_C; 2. DR Pfam; PF18072; FGAR-AT_linker; 1. DR Pfam; PF18076; FGAR-AT_N; 1. DR Pfam; PF22689; FGAR-AT_PurM_N-like; 1. DR Pfam; PF13507; GATase_5; 1. DR SMART; SM01211; GATase_5; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2. DR SUPFAM; SSF82697; PurS-like; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..1297 FT /note="Phosphoribosylformylglycinamidine synthase" FT /id="PRO_0000100412" FT DOMAIN 1043..1297 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT REGION 305..324 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1137 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT ACT_SITE 1262 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT ACT_SITE 1264 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT BINDING 307..318 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT BINDING 678 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT BINDING 679 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT BINDING 718 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT BINDING 722 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT BINDING 886 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" FT BINDING 888 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419" SQ SEQUENCE 1297 AA; 143043 MW; 9362706FEFE34CB4 CRC64; MLQIFRGSPA LSEFRLNQLA VRFQKANLPV SACYAEYIHF ADLSDRLTEE ETAKLDQLLH YGPTLAGHDP VGHCFIVIPR IGTISSWSSK ATDIAHNCGL NKVNRLERGL AFYFEFDRTL SSEEQQRLVS HIHDRMLEGI IHTPEEAKVL FDQQAPKPFT TVDILSGGRQ ALENANVELG LALAEDEIDY LVENFTALGR NPNDIELYMF AQANSEHCRH KIFNADWIID GEKQEKSLFK MIKNTFEKTP DHVLSAYKDN AAVMEGSKVG RFFPDQDGQY RYHNEDAHIL MKVETHNHPT AISPFPGAAT GSGGEIRDEG ATGRGAKPKA GLVGFSVSNL VIPGFEQPWE NPVSKPNRIA SALDIMIEGP LGGAAFNNEF GRPALLGYFR TYEEKVNSFA GEEVRGYHKP IMLAGGIGNI RAEHVQKGEI PVGAKLIVLG GPAMNIGLGG GAASSMASGK SKEDLDFASV QRDNPEMERR CQEVIDRCWQ LGEDNPILFI HDVGAGGLSN AMPELVHDGG RGGKFELRKI LSDERGMSPL EIWCNESQER YVLAVAPEKL ELFTALCERE RAPFAVIGEA TEQEHLTLHD DHFDNNPIDL PMNVLLGKTP KMTRDVKSKT VEGSALDHSQ IDLKEAFHRV LRLPVVAEKT FLITIGDRSV TGMVARDQMV GPWQIPVADC AVTTASLDSY HGEAMSMGER APVALLDFAA SARLAVAESI TNIAATNIGD IKRIKLSANW MSAAGHEGED AGLYQAVKAV GEELCPQLGL TIPVGKDSMS MKTTWHENGE QKTVTAPLSL VISAFARVED VRKTVTPQLR TDKGHSRLLL IDLGEGKNRL GATALAQVYK QLGDKPADVV NVESLKNFFN AMQALVAEQK LLAYHDRSDG GLIATLAEMA FAGNCGLSIH ISALGDNDLA VLFNEELGAV IQVRESDLSY VRDVLSQHGL IHLTKELGEV TTEDRIEISR GTKLLFSQKR SELRGIWAEL THQMQRLRDN PECADQEFAA KKDPENKGFS AHLTYDINED IAAPYIATGK KPRIAILREQ GVNSHYEMAA AFDRAGFEAI DVHMSDLHNA RYRLKDFNAL VACGGFSYGD VLGAGGGWAK SILFNPMLRD QFSEFFANPN TLTLGVCNGC QMVSNLAEII PGTDAWPRFV RNKSERFEAR AALVRINETN SLWFQGMAGS HMPIAVSHGE GRVEFKHDQQ LQMLKDQNLI VAQYIDNNLN PTEIYPANPN GSVEGITALS NQDGRVAIMM PHPERVFRTV SNSWHPEDWS EDGAWMRLFR NARVVLE //