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P08179 (PUR3_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoribosylglycinamide formyltransferase

EC=2.1.2.2
Alternative name(s):
5'-phosphoribosylglycinamide transformylase
GAR transformylase
Short name=GART
Gene names
Name:purN
Ordered Locus Names:b2500, JW2485
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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; 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.

Subunit structure

Monomer. Homodimer below pH 6.8. Ref.11

Sequence similarities

Belongs to the GART family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Phosphoribosylglycinamide formyltransferase
PRO_0000074943

Regions

Region11 – 1335'-phosphoribosylglycinamide binding
Region89 – 92410-formyltetrahydrofolate binding
Region140 – 144510-formyltetrahydrofolate binding
Region170 – 17345'-phosphoribosylglycinamide binding

Sites

Active site1081Proton donor Ref.6 Ref.8
Binding site64110-formyltetrahydrofolate
Binding site106110-formyltetrahydrofolate
Site1441Raises pKa of active site His

Experimental info

Mutagenesis701E → A: Loss of homodimerization. No effect on activity.
Mutagenesis1061N → A, D, G or S: Reduces activity about 2000-fold.
Mutagenesis1061N → E, H, I, K, L or Y: Loss of activity.
Mutagenesis1081H → A, G, M, N, Q or R: Loss of activity.
Mutagenesis1081H → E, S or T: Reduces activity about 1000-fold.
Mutagenesis1191H → A: No effect.
Mutagenesis1211H → Q: Increases Km for 5'-phosphoribosylglycinamide 4-fold.
Mutagenesis1351S → A or L: Reduces activity about 1000-fold.
Mutagenesis1371H → F or Q: No effect.
Mutagenesis1441D → A, E, S or Y: Reduces activity about 1000-fold.
Mutagenesis1441D → C, F, H, K, L, N, P, Q, R, T or V: Loss of activity.

Secondary structure

...................................... 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08179 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: D38F326BCBA103FB

FASTA21223,238
        10         20         30         40         50         60 
MNIVVLISGN GSNLQAIIDA CKTNKIKGTV RAVFSNKADA FGLERARQAG IATHTLIASA 

        70         80         90        100        110        120 
FDSREAYDRE LIHEIDMYAP DVVVLAGFMR ILSPAFVSHY AGRLLNIHPS LLPKYPGLHT 

       130        140        150        160        170        180 
HRQALENGDE EHGTSVHFVT DELDGGPVIL QAKVPVFAGD SEDDITARVQ TQEHAIYPLV 

       190        200        210 
ISWFADGRLK MHENAAWLDG QRLPPQGYAA DE 

« Hide

References

« Hide 'large scale' references
[1]"Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12."
Smith J.M., Daum H.A. III
J. Biol. Chem. 262:10565-10569(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Multiple independent origins of Shigella clones of Escherichia coli and convergent evolution of many of their characteristics."
Pupo G.M., Lan R., Reeves P.R.
Proc. Natl. Acad. Sci. U.S.A. 97:10567-10572(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ECOR 7.
[6]"Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase from Escherichia coli."
Inglese J., Smith J.M., Benkovic S.J.
Biochemistry 29:6678-6687(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, PARTIAL PROTEIN SEQUENCE.
[7]"A rapid screen of active site mutants in glycinamide ribonucleotide transformylase."
Warren M.S., Marolewski A.E., Benkovic S.J.
Biochemistry 35:8855-8862(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[8]"Catalytic mechanism of Escherichia coli glycinamide ribonucleotide transformylase probed by site-directed mutagenesis and pH-dependent studies."
Shim J.H., Benkovic S.J.
Biochemistry 38:10024-10031(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, ACTIVE SITE.
[9]"Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0-A resolution. A target enzyme for chemotherapy."
Chen P., Schulze-Gahmen U., Stura E.A., Inglese J., Johnson D.L., Marolewski A., Benkovic S.J., Wilson I.A.
J. Mol. Biol. 227:283-292(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[10]"Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase."
Almassy R.J., Janson C.A., Kan C.-C., Hostomska Z.
Proc. Natl. Acad. Sci. U.S.A. 89:6114-6118(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
[11]"A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A."
Su Y., Yamashita M.M., Greasley S.E., Mullen C.A., Shim J.H., Jennings P.A., Benkovic S.J., Wilson I.A.
J. Mol. Biol. 281:485-499(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-70 IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
[12]"New insights into inhibitor design from the crystal structure and NMR studies of Escherichia coli GAR transformylase in complex with beta-GAR and 10-formyl-5,8,10-trideazafolic acid."
Greasley S.E., Yamashita M.M., Cai H., Benkovic S.J., Boger D.L., Wilson I.A.
Biochemistry 38:16783-16793(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13747 Genomic DNA. Translation: AAA83899.1.
U00096 Genomic DNA. Translation: AAC75553.1.
AP009048 Genomic DNA. Translation: BAA16388.1.
AF293167 Genomic DNA. Translation: AAG14584.1.
PIRXYECGF. A28486.
RefSeqNP_416995.1. NC_000913.3.
YP_490728.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C2TX-ray2.10A/B1-212[»]
1C3EX-ray2.10A/B1-209[»]
1CDDX-ray2.80A/B1-212[»]
1CDEX-ray2.50A/B/C/D1-212[»]
1GARX-ray1.96A/B1-212[»]
1GRCX-ray3.00A/B1-212[»]
1JKXX-ray1.60A/B/C/D1-212[»]
2GARX-ray1.80A1-212[»]
3GARX-ray1.90A1-212[»]
ProteinModelPortalP08179.
SMRP08179. Positions 1-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08179. 1 interaction.
STRING511145.b2500.

Chemistry

BindingDBP08179.

Proteomic databases

PaxDbP08179.
PRIDEP08179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75553; AAC75553; b2500.
BAA16388; BAA16388; BAA16388.
GeneID12932446.
946973.
KEGGecj:Y75_p2453.
eco:b2500.
PATRIC32120389. VBIEscCol129921_2597.

Organism-specific databases

EchoBASEEB0792.
EcoGeneEG10799. purN.

Phylogenomic databases

eggNOGCOG0299.
HOGENOMHOG000033575.
KOK11175.
OMASPAFVAH.
OrthoDBEOG615VP4.
PhylomeDBP08179.

Enzyme and pathway databases

BioCycEcoCyc:GART-MONOMER.
ECOL316407:JW2485-MONOMER.
MetaCyc:GART-MONOMER.
RETL1328306-WGS:GSTH-1500-MONOMER.
UniPathwayUPA00074; UER00126.

Gene expression databases

GenevestigatorP08179.

Family and domain databases

Gene3D3.40.50.170. 1 hit.
InterProIPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR004607. PurN_trans.
[Graphical view]
PfamPF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF53328. SSF53328. 1 hit.
TIGRFAMsTIGR00639. PurN. 1 hit.
PROSITEPS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08179.
PROP08179.

Entry information

Entry namePUR3_ECOLI
AccessionPrimary (citable) accession number: P08179
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene