ID A0A2E5WMY1_UNCXX Unreviewed; 922 AA. AC A0A2E5WMY1; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 08-NOV-2023, entry version 20. DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01930}; DE EC=2.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01930}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|HAMAP-Rule:MF_01930}; DE AltName: Full=GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01930}; DE Short=GART {ECO:0000256|HAMAP-Rule:MF_01930}; GN Name=purN {ECO:0000256|HAMAP-Rule:MF_01930}; GN ORFNames=CL656_04765 {ECO:0000313|EMBL:MBI96438.1}; OS bacterium. OC Bacteria. OX NCBI_TaxID=1869227 {ECO:0000313|EMBL:MBI96438.1, ECO:0000313|Proteomes:UP000231188}; RN [1] {ECO:0000313|Proteomes:UP000231188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the RT Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 10- CC formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and CC tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D- CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)- CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide; CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366; CC EC=2.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01930}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; CC Evidence={ECO:0000256|ARBA:ARBA00023392}; 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 2/2. CC {ECO:0000256|ARBA:ARBA00004686}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)- CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1- CC diphosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005174}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)- CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D- CC ribosyl)glycinamide (10-formyl THF route): step 1/1. CC {ECO:0000256|ARBA:ARBA00005054, ECO:0000256|HAMAP-Rule:MF_01930}. CC -!- SIMILARITY: Belongs to the AIR synthase family. CC {ECO:0000256|ARBA:ARBA00010280}. CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|HAMAP- CC Rule:MF_01930}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family. CC {ECO:0000256|ARBA:ARBA00008630}. CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family. CC {ECO:0000256|ARBA:ARBA00007423}. CC -!- SIMILARITY: In the central section; belongs to the AIR synthase family. CC {ECO:0000256|ARBA:ARBA00008696}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBI96438.1}. 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; PBFJ01000026; MBI96438.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2E5WMY1; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000231188; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR CDD; cd08645; FMT_core_GART; 1. DR CDD; cd02196; PurM; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1. DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1. DR HAMAP; MF_01930; PurN; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR036477; Formyl_transf_N_sf. DR InterPro; IPR004607; GART. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf. DR InterPro; IPR020562; PRibGlycinamide_synth_N. 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 InterPro; IPR004733; PurM_cligase. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; TIGR00877; purD; 1. DR NCBIfam; TIGR00878; purM; 1. DR NCBIfam; TIGR00639; PurN; 1. DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1. DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01209; GARS_A; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF53328; Formyltransferase; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01930}; Transferase {ECO:0000256|HAMAP-Rule:MF_01930}. FT DOMAIN 109..313 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT ACT_SITE 826 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT BINDING 725..727 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT BINDING 782 FT /ligand="10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57454" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT BINDING 807..810 FT /ligand="10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57454" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT BINDING 824 FT /ligand="10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57454" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT SITE 865 FT /note="Raises pKa of active site His" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" SQ SEQUENCE 922 AA; 104878 MW; 62BFD649716EDC37 CRC64; MKILVVGCGG RENILIQKLK TNNTICCIGP WINPDIHKLC KYYLVTQINE YNVLNYCRVH SDIDYVVIGS ETLLETNFVN SCKQLNIKCI GPFRSLAQLE TSKYYTRLLL KESNYDCYNP KFNMISGEND IINIIDKYDK FVIKLNGLAG GKGVFVQDDH FKTREEGIKI IKQKIKEESI LIEEKLEGQE FSLFTLTDGY SSFHFPPVQD YKRAYDNDNG PNTGGMGSIM TDFDFLNEED IVKCEEINNN IIRIIQQKYN EPYIGILYGS FMMTNSKQIK LIEYNCRFGD SEVFNLLNSL ETDLSIIFKH MAEQRLNELR IEIKIHNSIV KYLVPPGYPN CSEKIKINYK PHNNVYAASI QNNILLGSRA IAVYGEGDTL DEAYNNCEEL IKKINYDNLY WRKDIGMRKD AYKMAGVDID KGNKFVSLIK DSVKSTYNEN VLGNYGSFGG QFKLNNNVLV ASTDGVGTKS ILIKKYKNNY YNCGIDIVNH SINDILVQGA KPLFFLDYIA SDKLDLNDST SFVEGCCVAC KKANCVLLGG ETAEMPTVYN KGHMDMVGTI VGEKVMNIET VQENDIAIGF SSSGPQTNGY TLIRKIMEKN RPSKIILNQL LSSHQSVLDQ INLIHSQFTI TGMCHITGGG LTENIKRTLP YDLNIPFDNI DYPLWCKWLK ENGNLSDDEM KKVFNCGIGF IVFVRPNETL TEFLIKNNLM NHKPLRIGIL GSTRGSNINA IYDAIYNNDT SFLYNKAEIV CTLSNKLNGG ILQRCQDLGI HNEYVPSKDY NKNDYDEKLI QIFENFNVDI ILCIGYMRIL TPIFTNKWKH KCFNVHPSLL PLFSGKMNLD VHKSVLEAGH DKTGCTIHEV TDDVDGGPII LQNMCPVYDN DTPEILKKRV QKLEQESLIE LLYNYIHLSG KVIYLNKVNK NI //