ID Q800F9_TETNG Unreviewed; 992 AA. AC Q800F9; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 22-FEB-2023, entry version 108. DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3 {ECO:0000256|ARBA:ARBA00021140}; DE EC=2.1.2.2 {ECO:0000256|ARBA:ARBA00012254}; DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047}; DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255}; GN Name=gart {ECO:0000313|EMBL:CAD67775.1}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAD67775.1}; RN [1] {ECO:0000313|EMBL:CAD67775.1} RP NUCLEOTIDE SEQUENCE. RA Lutfalla G., Roest Crollius H., Stange-Thomann N., Jaillon O., Mogensen K., RA Monneron D.; RT "Comparative genomic analysis reveals independent expansion of a lineage- RT specific gene family in vertebrates: The class II cytokine receptors and RT their ligands in mammals and fish."; RL BMC Genomics 4:29-29(2003). RN [2] {ECO:0000313|EMBL:CAF28785.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12869211; DOI=10.1186/1471-2164-4-29; RA Lutfalla G., Roest Crollius H., Stange-Thomann N., Jaillon O., Mogensen K., RA Monneron D.; RT "Comparative genomic analysis reveals independent expansion of a lineage- RT specific gene family in vertebrates: the class II cytokine receptors and RT their ligands in mammals and fish."; RL BMC Genomics 4:29-29(2003). RN [3] {ECO:0000313|EMBL:CAD67775.1} RP NUCLEOTIDE SEQUENCE. RA Lutfalla G.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. 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}. 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 --------------------------------------------------------------------------- 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; AJ544917; CAD67775.1; -; mRNA. DR EMBL; AJ544900; CAF28785.1; -; Genomic_DNA. DR AlphaFoldDB; Q800F9; -. DR UniPathway; UPA00074; UER00125. 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-EC. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. 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_00741; AIRS; 1. DR HAMAP; MF_00138; GARS; 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; IPR020559; PRibGlycinamide_synth_CS. 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 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; 2. 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 TIGRFAMs; TIGR00878; purM; 1. DR TIGRFAMs; TIGR00639; PurN; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. DR PROSITE; PS00373; GART; 1. PE 2: Evidence at transcript level; 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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}. FT DOMAIN 111..308 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT REGION 778..798 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 783..798 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 992 AA; 105017 MW; 1A9344E5B37EBBAC CRC64; MVAKVLVVGG GGREHALAWK LAQSPHLQQV LVAPGNAGTA DGGKISNSEV SVSNHAILAQ FCKDHQVGLV VVGPEAPLAA GIVDDLQAAG VPCFGPSAKA AQLEASKSFS KAFMERHGIP TARYGSFTDP QEACNFIRSA DFPALVVKAS GLAAGKGVVV AADRDEACRA VMDIMKIARL ERRERRWWWR SSWREKRCRV CASPTGPLWL PCLQRRTIRG CRTATGVPTP AVSQELLQQI RETVLQKTVD GMKAEGSPYV GVLYAGLMLT KQGPKVLEFN CRFGDPECQV LLPLLSSDLY EVIQNTLEGK LGSSAPVWRQ DSSAVTVVMA SSGYPGVYEK GVQITGLSQV QDMELQVFHA GTALRDGHVV SSGGRVLTVT AVRPALETAL QAANQGVAAI GFPGAVYRRD IGHRAIAHLK QRRGLTYKDS GVDIAAGNKL VDMIKPLAKA TSRAGCNAEL GGFAGLFDLK AAGFVDPILV SGTDGVGTKL KISQACGQHA SLGQDLVAMC VNDVLAQGAE PLFFLDYFSC GSLDVDVAAS VIDGIAKACK MAGCALLGGE TAEMPGVYGP GEYDLAGFCV GAVERGALLP RISDISEGDL LIGVASSGVH SNGFSLVRKV LERAGLSYSS PSPFGASGQT IGEVLLTPTK IYSRLMLPIL RSGAVKAYAH ITGGGLLENI PRVLPQELLV DIDASQWSVP PVFSWLYKEG GLSELEMART FNCGLGAVLV VSPVDAQMIL HQLRAEEQAW IVGSLVRKQP GAEPVMVRNL KRSLLKAEPA SSEATAAKQS GSTPHRRTKV GTNLQALIDQ ARRPSSSAEI VVVVSNRPGV QGLKRAALAG IPTRVVDHKL FGSRAEFDST INAVLEEFGV ELVCLAGFMR ILTGTFVRKW NGKLLNIHPS LLPSFKGVNA QKQALQAGVR VAGCTVHFVA EEVDAGAIIV QEAVPVLVGD TEDSLSDRIK EAEHRAFPSA LELVASGTVC LGKDGHIEWK AP //