ID PUR3_STAAN Reviewed; 188 AA. AC P99162; Q99V25; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 112. DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01930}; DE EC=2.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01930}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000255|HAMAP-Rule:MF_01930}; DE AltName: Full=GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01930}; DE Short=GART {ECO:0000255|HAMAP-Rule:MF_01930}; GN Name=purN {ECO:0000255|HAMAP-Rule:MF_01930}; OrderedLocusNames=SA0924; OS Staphylococcus aureus (strain N315). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N315; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=N315; RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017; RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.; RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus RT aureus during the post-exponential phase of growth."; RL J. Microbiol. Methods 60:247-257(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=N315; RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.; RT "Shotgun proteomic analysis of total and membrane protein extracts of S. RT aureus strain N315."; RL Submitted (OCT-2007) to UniProtKB. 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:0000255|HAMAP-Rule:MF_01930}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(1)-(5-phospho-beta-D-ribosyl)glycinamide + (6R)-10- CC formyltetrahydrofolate = N(2)-formyl-N(1)-(5-phospho-beta-D- CC ribosyl)glycinamide + (6S)-5,6,7,8-tetrahydrofolate + H(+); 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:0000255|HAMAP-Rule:MF_01930}; 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:0000255|HAMAP-Rule:MF_01930}. CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000255|HAMAP- CC Rule:MF_01930}. 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; BA000018; BAB42169.1; -; Genomic_DNA. DR PIR; F89876; F89876. DR RefSeq; WP_000238669.1; NC_002745.2. DR AlphaFoldDB; P99162; -. DR SMR; P99162; -. DR EnsemblBacteria; BAB42169; BAB42169; BAB42169. DR KEGG; sau:SA0924; -. DR HOGENOM; CLU_038395_1_3_9; -. DR UniPathway; UPA00074; UER00126. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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 CDD; cd08645; FMT_core_GART; 1. DR FunFam; 3.40.50.170:FF:000014; Phosphoribosylglycinamide formyltransferase; 1. DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1. DR HAMAP; MF_01930; PurN; 1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR036477; Formyl_transf_N_sf. DR InterPro; IPR004607; GART. DR NCBIfam; TIGR00639; PurN; 1. DR PANTHER; PTHR43369; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1. DR PANTHER; PTHR43369:SF2; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF53328; Formyltransferase; 1. PE 1: Evidence at protein level; KW Purine biosynthesis; Transferase. FT CHAIN 1..188 FT /note="Phosphoribosylglycinamide formyltransferase" FT /id="PRO_0000074947" FT ACT_SITE 110 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930" FT BINDING 12..14 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930" FT BINDING 66 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930" FT BINDING 91..94 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930" FT BINDING 108 FT /ligand="(6R)-10-formyltetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:195366" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930" FT SITE 146 FT /note="Raises pKa of active site His" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930" SQ SEQUENCE 188 AA; 21166 MW; F0364618F275FA30 CRC64; MVKIAIFASG SGSNFENIVE HVESGKLENI EVTALYTDHQ NAFCIDRAKK HDIPVYINEP KQFDSKAAYE QHLVTLLNKD KVEWIILAGY MRLIGPDLLA SFEGKILNIH PSLLPKYKGI DAIGQAYHSG DTITGSTVHY VDCGMDTGEI IEQRQCDIRP DDSKEQLEEK VKKLEYELYP SVIAKIVK //