ID Q2GH93_EHRCR Unreviewed; 208 AA. AC Q2GH93; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 26-FEB-2020, entry version 80. 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 ECO:0000313|EMBL:ABD44645.1}; GN OrderedLocusNames=ECH_0370 {ECO:0000313|EMBL:ABD44645.1}; OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=205920 {ECO:0000313|EMBL:ABD44645.1, ECO:0000313|Proteomes:UP000008320}; RN [1] {ECO:0000313|EMBL:ABD44645.1, ECO:0000313|Proteomes:UP000008320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC CRL-10679 / Arkansas {ECO:0000313|Proteomes:UP000008320}; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). 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=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-D- CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)- CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, CC ChEBI:CHEBI:58426, ChEBI:CHEBI:58457; EC=2.1.2.2; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01930}. CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|HAMAP- CC Rule:MF_01930}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP000236; ABD44645.1; -; Genomic_DNA. DR RefSeq; WP_006009991.1; NC_007799.1. DR STRING; 205920.ECH_0370; -. DR EnsemblBacteria; ABD44645; ABD44645; ECH_0370. DR KEGG; ech:ECH_0370; -. DR eggNOG; ENOG4108V3E; Bacteria. DR eggNOG; COG0299; LUCA. DR HOGENOM; CLU_038395_1_1_5; -. DR KO; K11175; -. DR OMA; TGITIHY; -. DR OrthoDB; 1815747at2; -. DR BioCyc; ECHA205920:G1G5L-301-MONOMER; -. DR UniPathway; UPA00074; UER00126. DR Proteomes; UP000008320; Chromosome. 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 HAMAP; MF_01930; PurN; 1. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR036477; Formyl_transf_N_sf. DR InterPro; IPR004607; GART. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR TIGRFAMs; TIGR00639; PurN; 1. PE 3: Inferred from homology; KW Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01930}; KW Reference proteome {ECO:0000313|Proteomes:UP000008320}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01930, ECO:0000313|EMBL:ABD44645.1}. FT DOMAIN 5..179 FT /note="Formyl_trans_N" FT /evidence="ECO:0000259|Pfam:PF00551" FT REGION 14..16 FT /note="5'-phosphoribosylglycinamide binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT ACT_SITE 106 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT BINDING 62 FT /note="10-formyltetrahydrofolate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT BINDING 104 FT /note="10-formyltetrahydrofolate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" FT SITE 142 FT /note="Raises pKa of active site His" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930" SQ SEQUENCE 208 AA; 22811 MW; 555CA2CFE2600229 CRC64; MTPLKLGILI SGRGSNMQAL INACAQDDFP AEVSCVISNN PKANGLLIAQ KQNIKTFVVQ GRPLDFDSID SILRQHQVDL ICLAGFMSIV PEGFINKWFH KIINIHPSLL PSFKGLNAQS QALKAGVKIA GCTVHYVYPE VDGGPIIVQA AVPVFSSDNL TDLSERILKM EHICYPKAVK LIALNQLQLN ENLATSAELL HMFYDETI //