ID A0A6L7GIU3_9ACTN Unreviewed; 621 AA. AC A0A6L7GIU3; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 13-SEP-2023, entry version 14. DE RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01643}; DE EC=6.3.1.21 {ECO:0000256|HAMAP-Rule:MF_01643}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643}; DE AltName: Full=Formate-dependent GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01643}; DE AltName: Full=GAR transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643}; DE Short=GART 2 {ECO:0000256|HAMAP-Rule:MF_01643}; DE AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000256|HAMAP-Rule:MF_01643}; DE AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000256|HAMAP-Rule:MF_01643}; GN Name=purT {ECO:0000256|HAMAP-Rule:MF_01643, GN ECO:0000313|EMBL:MXP19859.1}; GN ORFNames=GIY30_00580 {ECO:0000313|EMBL:MXP19859.1}; OS Gordonia mangrovi. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae; OC Gordonia. OX NCBI_TaxID=2665643 {ECO:0000313|EMBL:MXP19859.1, ECO:0000313|Proteomes:UP000475545}; RN [1] {ECO:0000313|EMBL:MXP19859.1, ECO:0000313|Proteomes:UP000475545} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HNM0687 {ECO:0000313|EMBL:MXP19859.1, RC ECO:0000313|Proteomes:UP000475545}; RA Huang X., Xie Y., Chu X., Xiao K.; RT "Gordonia sp. nov., a novel actinobacterium isolated from mangrove soil in RT Hainan."; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the CC transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing CC 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by CC PurU via hydrolysis of 10-formyl-tetrahydrofolate. {ECO:0000256|HAMAP- CC Rule:MF_01643}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = CC ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + CC phosphate; Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:456216; CC EC=6.3.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01643}; 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 (formate route): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01643}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01643}. CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP- CC Rule:MF_01643}. 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:MXP19859.1}. 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; WMBR01000001; MXP19859.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6L7GIU3; -. DR UniPathway; UPA00074; UER00127. DR Proteomes; UP000475545; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. 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 HAMAP; MF_01643; PurT; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003135; ATP-grasp_carboxylate-amine. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR InterPro; IPR005862; PurT. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; TIGR01142; purT; 1. DR PANTHER; PTHR43055; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1. DR PANTHER; PTHR43055:SF1; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1. DR Pfam; PF02222; ATP-grasp; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01643}; Ligase {ECO:0000256|HAMAP-Rule:MF_01643}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01643}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01643}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_01643}; Reference proteome {ECO:0000313|Proteomes:UP000475545}; KW Transferase {ECO:0000313|EMBL:MXP19859.1}. FT DOMAIN 187..387 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT REGION 1..72 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 477..621 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 480..605 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 89..90 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 149 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 223 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 228..233 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 263..266 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 346 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 358 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 365 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 434 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" FT BINDING 441..442 FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide" FT /ligand_id="ChEBI:CHEBI:143788" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643" SQ SEQUENCE 621 AA; 63779 MW; DD83B872308EF436 CRC64; MTSESDNASQ ASAPAGGEAA SAPDAQAPTP AEHAVPAEQA PAAQAPADQQ QEDRGPGQAV PAPAVGPPAV IGTPLSPSAT KVMVLGAGEL GKEVIIAFQR LGVEVIAVDR YADAPGQQVA HHAEVIDMTD PAALLALIER YRPHYVVPEI EAIATEALIE VEKRALAEVI PTAHAVVATM NREGIRRLAD EELGLPTSPY LFASSAEDLE AAVAEIGFPC VVKPVMSSSG KGQTVVRAPA DIGTAWENAT TGARVQGERV IVEGFIEFDY EITLLTVRAI DPVTGRLASH FCAPIGHQQV GGDYVESWQP HEMSADALAA ATSIAARIAT AMGDGKLGGR GIFGVELFVQ GDDVYFSEVS PRPHDTGLVT LATQRLSEFE MHARAILGLP VDVTLASPGA SAVIYGQLDE PAIGFSNVAR ALAVPETDIR LFGKPQSFHR RRMGVITATA DDVATARQRA VQAASLVTPV AARPFERAVP EPLGNPPVPP PPRRPGPPPQ GAPTPPAPGG PQRPHQPGGG YPGGPPRPGG PPMPGQPPRP GPGGRPPQGA PPGPPPGGPR PGPPPMRGPQ PPRGGAPGRP AGPPPGRPSP PPPGPTPPPV SHPVGPSANR PADEPSRASV D //