ID PUR2_CHITE Reviewed; 1371 AA. AC Q26255; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=Trifunctional purine biosynthetic protein adenosine-3; DE Includes: DE RecName: Full=Phosphoribosylamine--glycine ligase; DE EC=6.3.4.13; DE AltName: Full=Glycinamide ribonucleotide synthetase; DE Short=GARS; DE AltName: Full=Phosphoribosylglycinamide synthetase; DE Includes: DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase; DE EC=6.3.3.1; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase; DE AltName: Full=AIR synthase; DE Short=AIRS; DE Includes: DE RecName: Full=Phosphoribosylglycinamide formyltransferase; DE EC=2.1.2.2; DE AltName: Full=5'-phosphoribosylglycinamide transformylase; DE AltName: Full=GAR transformylase; DE Short=GART; GN Name=GART; OS Chironomus tentans (Midge). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; OC Chironomidae; Chironominae; Chironomus. OX NCBI_TaxID=7153; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92389368; PubMed=1518084; DOI=10.1007/BF00160260; RA Clark D.V., Henikoff S.; RT "Unusual organizational features of the Drosophila Gart locus are not RT conserved within Diptera."; RL J. Mol. Evol. 35:51-59(1992). CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D- CC ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole. CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + N(1)-(5-phospho-D- CC ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)- CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 2/2. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5- CC phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family. CC -!- SIMILARITY: In the central section; belongs to the AIR synthase CC family. CC -!- SIMILARITY: In the C-terminal section; belongs to the GART family. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S43653; AAB23115.1; -; Genomic_DNA. DR HSSP; P22102; 1NJS. DR BRENDA; 2.1.2.2; 275797. DR BRENDA; 6.3.3.1; 275797. DR BRENDA; 6.3.4.13; 275797. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:EC. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-lig...; IEA:EC. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase...; IEA:EC. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro. DR GO; GO:0009113; P:purine base biosynthetic process; IEA:InterPro. DR InterPro; IPR000728; AIR_synth. DR InterPro; IPR010918; AIR_synth_C. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR002376; Formyl_transf_N. DR InterPro; IPR000115; Gars. DR InterPro; IPR001555; GART_AS. DR InterPro; IPR013817; Pre-ATP_grasp. DR InterPro; IPR004733; PurM_cligase. DR InterPro; IPR004607; PurN_trans. DR Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR Gene3D; G3DSA:3.40.50.170; Formyl_transf_N; 1. DR Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1. DR Pfam; PF00586; AIRS; 2. DR Pfam; PF02769; AIRS_C; 2. 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 TIGRFAMs; TIGR00877; purD; 1. DR TIGRFAMs; TIGR00878; purM; 2. DR TIGRFAMs; TIGR00639; PurN; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. DR PROSITE; PS00373; GART; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Manganese; Metal-binding; Multifunctional enzyme; KW Nucleotide-binding; Purine biosynthesis; Transferase. FT CHAIN 1 1371 Trifunctional purine biosynthetic protein FT adenosine-3. FT /FTId=PRO_0000074933. FT DOMAIN 115 321 ATP-grasp. FT NP_BIND 141 202 ATP (By similarity). FT REGION 434 1171 AIRS. FT REGION 1172 1371 GART. FT REGION 1180 1182 5'-phosphoribosylglycinamide binding (By FT similarity). FT REGION 1260 1263 10-formyltetrahydrofolate binding (By FT similarity). FT REGION 1311 1315 10-formyltetrahydrofolate binding (By FT similarity). FT REGION 1341 1344 5'-phosphoribosylglycinamide binding (By FT similarity). FT ACT_SITE 1279 1279 Proton donor (By similarity). FT METAL 291 291 Manganese (By similarity). FT METAL 293 293 Manganese (By similarity). FT BINDING 1235 1235 10-formyltetrahydrofolate (By FT similarity). FT BINDING 1277 1277 10-formyltetrahydrofolate (By FT similarity). FT SITE 1315 1315 Raises pKa of active site His (By FT similarity). SQ SEQUENCE 1371 AA; 149103 MW; 7BF4664DB1538946 CRC64; MTGKKLLLIG SGGREHALAW KLQQSKNVTE IFAFPGSIGI SQLEKVQLVN NNEMNLKDFK GIASWCKINH IDLVIVGPED PLAEGIADQL KAANIHCFGP SKAGARIESD KSWSKDFMIR HHIPTAQYGS FIDALKAKDF IRNTPNALVV KASGLAAGKG VIVAENIEEA CAAVDEILGD HKFGTAGDVV VVEEKLSGQE VSVLGFVDSN SVRILPPAQD HKRLKDNDEG LNTGGMGAYC PCPLISQQEL DIVKSQVLQR AVDGLRKENI LYNGILYAGI MLTHDGPKTL EFNCRFGDPE TQIILPLLDE DLYDLMMASC TNHLCNVPEL KFKSNINAVG VVMASKGYPE TSTKGCVISG IESVETMDNH IVFHSGTSKN NKDEWITNGG RVLINIALAD NLKKAADLAT KACDVVKFDG SQYRRDIGKK AFQIHSLTYK ESGVNIEAGN SLVGRIKSLS YGTHRSGVVG QIGSFGGLMR LNDIKYINSN GEESNYKDIV LVQGTDGVGT KLKIAESMNV WDTIGIDLVA MCVNDVLCNG AEPIGFLDYI ACGHLEVPTV ATIVKGIADG CRKANCALIG GETAEMPSMY GKGKYDLAGY CVGITEYDEI LPKINDVHVG DVVIGLPSSG IHSNGFSLVN KIFQQTGFKL TDIAEFSDSH KSYGMEFLTP TRLYVSETLP FLRNGYVKAL AHITGGGLLE NIPRILPNHL SVQIDALTWK LPKVFSWLAA HGNVNANEML RTFNCGIGMI IIMPRNDIEW ETIPEARMIG SITQRDHNGP QVIVKNFKEV LHKEVTHWKK GDAETTSISY KDSGVDITAG NELVDNIKPH AKSTNRKGVI GGLGSFGGLF RINECGTKFE DPMLVLATDG VGTKLKIAQQ LGKHDTVGID LVAMCNNDIL CNGAEPLTFL DYFACGKLDV NVATNVVSGI AEGCRQSDST LLGGETAEMP GMYNPNVYDL AGFSLGVAEH EDILPKKNCL EVGDIIIGFP SNGVHSNGFS LIHKLFELTG YKWTDIAPFS AYGKTFGEEF LEPTKVYVKE ISPALKTGYV KALAHITGGG LWDNIPRVLP YNLTAELDAK KINISPVFAW LSLNGNIDKL ELLKTFNCGI GMIMIASKEH ELEILKSLYG SRASVIGKII PTKPHGHQVI VRHFATCFER VERLLSIPKK RVGVLISGSG SNLQALIDAT KSTNMGMCSE IVFVLSNKAG IFGLERAAKA NIPSTVISNK DYATREAFDV ALHNELIKHN VEIICLAGFM RILTPCFVNK WKGKLLNIHP SLLPKYKGIT AQKDALESGD NESGCTVHFV DENVDTGAII VQEIVPIFEN DTVESLTERI HVAEHIAFPK ALRLVASGYV RLNDKCETEW A //