ID A0A6H5GGT2_9HEMI Unreviewed; 1406 AA. AC A0A6H5GGT2; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 03-AUG-2022, entry version 7. DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3 {ECO:0000256|RuleBase:RU363089}; DE Includes: DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|RuleBase:RU363089}; DE EC=6.3.4.13 {ECO:0000256|RuleBase:RU363089}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|RuleBase:RU363089}; DE Short=GARS {ECO:0000256|RuleBase:RU363089}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|RuleBase:RU363089}; DE Includes: DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|RuleBase:RU363089}; DE EC=6.3.3.1 {ECO:0000256|RuleBase:RU363089}; DE AltName: Full=AIR synthase {ECO:0000256|RuleBase:RU363089}; DE Short=AIRS {ECO:0000256|RuleBase:RU363089}; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|RuleBase:RU363089}; DE Includes: DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|RuleBase:RU363089}; DE EC=2.1.2.2 {ECO:0000256|RuleBase:RU363089}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|RuleBase:RU363089}; DE AltName: Full=GAR transformylase {ECO:0000256|RuleBase:RU363089}; DE Short=GART {ECO:0000256|RuleBase:RU363089}; GN ORFNames=NTEN_LOCUS7682 {ECO:0000313|EMBL:CAB0001895.1}; OS Nesidiocoris tenuis. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; OC Cimicomorpha; Miridae; Dicyphina; Nesidiocoris. OX NCBI_TaxID=355587 {ECO:0000313|EMBL:CAB0001895.1, ECO:0000313|Proteomes:UP000479000}; RN [1] {ECO:0000313|EMBL:CAB0001895.1, ECO:0000313|Proteomes:UP000479000} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Ferguson B K.; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-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:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286; CC EC=2.1.2.2; Evidence={ECO:0000256|RuleBase:RU363089}; 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|RuleBase:RU363089}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; CC Evidence={ECO:0000256|RuleBase:RU363089}; 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, ECO:0000256|RuleBase:RU363089}. 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 ECO:0000256|RuleBase:RU363089}. 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|RuleBase:RU363089}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family. CC {ECO:0000256|ARBA:ARBA00008630, ECO:0000256|RuleBase:RU363089}. CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family. CC {ECO:0000256|ARBA:ARBA00007423, ECO:0000256|RuleBase:RU363089}. CC -!- SIMILARITY: In the central section; belongs to the AIR synthase family. CC {ECO:0000256|ARBA:ARBA00008696, ECO:0000256|RuleBase:RU363089}. 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; CADCXU010011729; CAB0001895.1; -; Genomic_DNA. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000479000; 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-UniRule. 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:0004672; F:protein kinase activity; IEA:InterPro. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd08645; FMT_core_GART; 1. DR CDD; cd02196; PurM; 1. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.90.600.10; -; 1. DR Gene3D; 3.90.650.10; -; 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; IPR011009; Kinase-like_dom_sf. 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; IPR000719; Prot_kinase_dom. 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 InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR10520; PTHR10520; 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 Pfam; PF00069; Pkinase; 1. DR SMART; SM01210; GARS_C; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR SUPFAM; SSF53328; SSF53328; 1. DR SUPFAM; SSF55326; SSF55326; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR TIGRFAMs; TIGR00877; purD; 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. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Coiled coil {ECO:0000256|SAM:Coils}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363089}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU363089}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU363089}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, KW ECO:0000256|RuleBase:RU363089}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, KW ECO:0000256|RuleBase:RU363089}; KW Reference proteome {ECO:0000313|Proteomes:UP000479000}. FT DOMAIN 119..408 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 516..723 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT REGION 77..139 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 375..412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 165..199 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 77..97 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1406 AA; 152244 MW; 4FDB2C9478C2893E CRC64; MEQHKAHTNK CIDFVKKLLK EKSNIEKKEA RQRCMQNRLR LGQFVTQRVG ATFQENWTDG YAFQELSRRQ EEIAAEREEI DRQKKLLTKK RPTNSETGRG KRSGSSGGAG GAGSGGNSLP GGGGAGAGSQ AVLHNGTDTF LKPDPVPTMS AQEYYEADEI LKLRQSALKK EDADLQLEME KLERERNLHI RELKRIHNED QSRFNNHPVL NDRYLLLMLL GKGGFSEVHK HKTIAEREAR SIVMQVVSAL KYLNEIKPPV IHYDLKPGNI LLTEGNVCGE IKITDFGLSK VMDEENYNPD HGMDLTSQGA GTYCPKMSAK RHQLRIIMTR TRKLSHTIPV RVLATDPCQS LHLIVDRRRN VLVQGRDHDR RVARALASRS TGPALDRPAA HPARRTARPR AVTRAPGAAR TRHTGAGGAL ILEAPSRIVG DTTAPGYAGI QILRDDRYGR RRYDELPFSY CALCDWSITQ CINLVVVGPE APLENGIADA FTDAGIPCFG PRACAARIET DKEFAKEFMV RHGIPTARFK SFQAADDAKK FIRSSDFKAL VVKASGIAAG KGVIVAKDVD EACAAVDSML IERKFGEAGS TVVVEEVLEG EEVSVLAFSD GVHTKVMLPA QDHKRVFDED QGANTGGMGA YAPCPLVDSS MLSWIATNVI QKAINGLRKE NKPFVGCLFA GLMMTSDGPK VLEYNCRFGD PETEVLLPLL RSNLFTTMMA CCRGTLDLVD LEWEQGVCCV GVVMSSRGYP ESSSKGDLIE GLEEVQKWKE ITTFHAGTAK TNGKWVTNGG RVLINVAKSP SLVKAANLAT SACQFITIPG GHFRKDIAHK GIPRWILNQG AMSYKKSGVD IEAGEALVSS IVPSVNETKR AGVLSHLGGF GAFFDPALSG FKNPILVSGT DGVGTKLKVA QAVGNHNTIG IDLVAMCVND ILCHGAEPLF FLDYFACGHL EVEVAAQVVK GVTEGCKLSG CALVGGETAE MPGLYGPGDY DLAGFAVGAV EKGSELPRVK SIVENDVVIA LPSSGVHSNG LSLARKIVEK QGLRFSDKAP FSNQTIGNEL LTPTRIYVQE VLPVVKTGKI KAIAHITGGG LTENIIRVLP DEMRVVLDAT KWKIPPIFPW LSAVGDISES EMLRTFNCGV GLVLIASPGN ADDVVKAIKS SSIVGSVAKK SPSEKGVLVN GLSSAFSPLM KPHIPHIIQQ EAKKKRIGVL ISGSGTNLQS LIDSVADGRI NGEIVLVISN KTGVQGLSRA EKAGIPSIVI PHTKFPTREA FEEDVHNHLL AARVDLVVLA GFMRVLTGWF VSRWRGKIIN VHPSLLPSFK GVNAWQQALD AGVAVSGCTV HYVEEDIDNG AIIAQGVVPV SPNETVTSLQ DKIRVEEHKA LSRAVQLICS GSAVLDLVSN KIVWRH //