Reviewed, UniProtKB/Swiss-Prot Q26255 (PUR2_CHITE)

Names and origin

Protein names

Recommended name:
    Trifunctional purine biosynthetic protein adenosine-3
Including the following 3 domains:
    1- Recommended name:
            Phosphoribosylamine--glycine ligase
              EC=6.3.4.13
        Alternative name(s):
            Glycinamide ribonucleotide synthetase
              Short name=GARS
            Phosphoribosylglycinamide synthetase
    2- Recommended name:
            Phosphoribosylformylglycinamidine cyclo-ligase
              EC=6.3.3.1
        Alternative name(s):
            Phosphoribosyl-aminoimidazole synthetase
            AIR synthase
              Short name=AIRS
    3- Recommended name:
            Phosphoribosylglycinamide formyltransferase
              EC=2.1.2.2
        Alternative name(s):
            5'-phosphoribosylglycinamide transformylase
            GAR transformylase
              Short name=GART

Gene names

Name:

GART

Organism

Chironomus tentans (Midge)

Taxonomic identifier

7153 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Chironomoidea › Chironomidae › Chironominae › Chironomus

Protein attributes

Sequence length	1371 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. 10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5. Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Sequence similarities	In the N-terminal section; belongs to the GARS family. In the central section; belongs to the AIR synthase family. In the C-terminal section; belongs to the GART family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro purine base biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosylamine-glycine ligase activity Inferred from electronic annotation. Source: EC phosphoribosylformylglycinamidine cyclo-ligase activity Inferred from electronic annotation. Source: EC phosphoribosylglycinamide formyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1371	1371	Trifunctional purine biosynthetic protein adenosine-3		PRO_0000074933
Regions
	Domain	115 – 321	207	ATP-grasp
	Nucleotide binding	141 – 202	62	ATP By similarity
	Region	434 – 1171	738	AIRS
	Region	1172 – 1371	200	GART
	Region	1180 – 1182	3	5'-phosphoribosylglycinamide binding By similarity
	Region	1260 – 1263	4	10-formyltetrahydrofolate binding By similarity
	Region	1311 – 1315	5	10-formyltetrahydrofolate binding By similarity
	Region	1341 – 1344	4	5'-phosphoribosylglycinamide binding By similarity
Sites
	Active site	1279	1	Proton donor By similarity
	Metal binding	291	1	Manganese By similarity
	Metal binding	293	1	Manganese By similarity
	Binding site	1235	1	10-formyltetrahydrofolate By similarity
	Binding site	1277	1	10-formyltetrahydrofolate By similarity
	Site	1315	1	Raises pKa of active site His By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q26255-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7BF4664DB1538946	FASTA	1,371	149,103
	10 20 30 40 50 60 MTGKKLLLIG SGGREHALAW KLQQSKNVTE IFAFPGSIGI SQLEKVQLVN NNEMNLKDFK 70 80 90 100 110 120 GIASWCKINH IDLVIVGPED PLAEGIADQL KAANIHCFGP SKAGARIESD KSWSKDFMIR 130 140 150 160 170 180 HHIPTAQYGS FIDALKAKDF IRNTPNALVV KASGLAAGKG VIVAENIEEA CAAVDEILGD 190 200 210 220 230 240 HKFGTAGDVV VVEEKLSGQE VSVLGFVDSN SVRILPPAQD HKRLKDNDEG LNTGGMGAYC 250 260 270 280 290 300 PCPLISQQEL DIVKSQVLQR AVDGLRKENI LYNGILYAGI MLTHDGPKTL EFNCRFGDPE 310 320 330 340 350 360 TQIILPLLDE DLYDLMMASC TNHLCNVPEL KFKSNINAVG VVMASKGYPE TSTKGCVISG 370 380 390 400 410 420 IESVETMDNH IVFHSGTSKN NKDEWITNGG RVLINIALAD NLKKAADLAT KACDVVKFDG 430 440 450 460 470 480 SQYRRDIGKK AFQIHSLTYK ESGVNIEAGN SLVGRIKSLS YGTHRSGVVG QIGSFGGLMR 490 500 510 520 530 540 LNDIKYINSN GEESNYKDIV LVQGTDGVGT KLKIAESMNV WDTIGIDLVA MCVNDVLCNG 550 560 570 580 590 600 AEPIGFLDYI ACGHLEVPTV ATIVKGIADG CRKANCALIG GETAEMPSMY GKGKYDLAGY 610 620 630 640 650 660 CVGITEYDEI LPKINDVHVG DVVIGLPSSG IHSNGFSLVN KIFQQTGFKL TDIAEFSDSH 670 680 690 700 710 720 KSYGMEFLTP TRLYVSETLP FLRNGYVKAL AHITGGGLLE NIPRILPNHL SVQIDALTWK 730 740 750 760 770 780 LPKVFSWLAA HGNVNANEML RTFNCGIGMI IIMPRNDIEW ETIPEARMIG SITQRDHNGP 790 800 810 820 830 840 QVIVKNFKEV LHKEVTHWKK GDAETTSISY KDSGVDITAG NELVDNIKPH AKSTNRKGVI 850 860 870 880 890 900 GGLGSFGGLF RINECGTKFE DPMLVLATDG VGTKLKIAQQ LGKHDTVGID LVAMCNNDIL 910 920 930 940 950 960 CNGAEPLTFL DYFACGKLDV NVATNVVSGI AEGCRQSDST LLGGETAEMP GMYNPNVYDL 970 980 990 1000 1010 1020 AGFSLGVAEH EDILPKKNCL EVGDIIIGFP SNGVHSNGFS LIHKLFELTG YKWTDIAPFS 1030 1040 1050 1060 1070 1080 AYGKTFGEEF LEPTKVYVKE ISPALKTGYV KALAHITGGG LWDNIPRVLP YNLTAELDAK 1090 1100 1110 1120 1130 1140 KINISPVFAW LSLNGNIDKL ELLKTFNCGI GMIMIASKEH ELEILKSLYG SRASVIGKII 1150 1160 1170 1180 1190 1200 PTKPHGHQVI VRHFATCFER VERLLSIPKK RVGVLISGSG SNLQALIDAT KSTNMGMCSE 1210 1220 1230 1240 1250 1260 IVFVLSNKAG IFGLERAAKA NIPSTVISNK DYATREAFDV ALHNELIKHN VEIICLAGFM 1270 1280 1290 1300 1310 1320 RILTPCFVNK WKGKLLNIHP SLLPKYKGIT AQKDALESGD NESGCTVHFV DENVDTGAII 1330 1340 1350 1360 1370 VQEIVPIFEN DTVESLTERI HVAEHIAFPK ALRLVASGYV RLNDKCETEW A

References

[1]	"Unusual organizational features of the Drosophila Gart locus are not conserved within Diptera." Clark D.V., Henikoff S. J. Mol. Evol. 35:51-59(1992) [PubMed: 1518084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	S43653 Genomic DNA. Translation: AAB23115.1.
3D structure databases
HSSP	HSSP built from PDB template 1NJS based on UniProtKB P22102.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.1.2.2. 275797. 6.3.3.1. 275797. 6.3.4.13. 275797.
Family and domain databases
InterPro	IPR000728. AIR_synth. IPR010918. AIR_synth_C. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR002376. Formyl_transf_N. IPR000115. Gars. IPR001555. GART_AS. IPR013817. Pre-ATP_grasp. IPR004733. PurM_cligase. IPR004607. PurN_trans. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.170. Formyl_transf_N. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF00586. AIRS. 2 hits. PF02769. AIRS_C. 2 hits. PF00551. Formyl_trans_N. 1 hit. PF01071. GARS_A. 1 hit. PF02843. GARS_C. 1 hit. PF02844. GARS_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00877. purD. 1 hit. TIGR00878. purM. 2 hits. TIGR00639. PurN. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00184. GARS. 1 hit. PS00373. GART. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR2_CHITE

Accession

Primary (citable) accession number: Q26255

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)