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P08179

- PUR3_ECOLI

UniProt

P08179 - PUR3_ECOLI

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Protein

Phosphoribosylglycinamide formyltransferase

Gene

purN

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.2 PublicationsUniRule annotation

Catalytic activityi

10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.2 PublicationsUniRule annotation

Enzyme regulationi

Inhibited by N10-(bromoacetyl)-5,8-dideazafolate.1 Publication

Kineticsi

kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 7.5).1 Publication

  1. KM=77.5 µM for (6R)-N10-formyltetrahydrofolate (at pH 8.5)1 Publication
  2. KM=84.8 µM for (6R)-N10-formyltetrahydrofolate (at pH 7.5)1 Publication

pH dependencei

Optimum pH is 8.51 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 64110-formyltetrahydrofolate1 PublicationUniRule annotation
Binding sitei106 – 106110-formyltetrahydrofolate1 PublicationUniRule annotation
Active sitei108 – 1081Proton donor1 PublicationUniRule annotation
Sitei144 – 1441Raises pKa of active site His1 PublicationUniRule annotation

GO - Molecular functioni

  1. methyltransferase activity Source: InterPro
  2. phosphoribosylglycinamide formyltransferase activity Source: EcoCyc

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. cellular response to DNA damage stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:GART-MONOMER.
ECOL316407:JW2485-MONOMER.
MetaCyc:GART-MONOMER.
RETL1328306-WGS:GSTH-1500-MONOMER.
UniPathwayiUPA00074; UER00126.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylglycinamide formyltransferaseUniRule annotation (EC:2.1.2.22 PublicationsUniRule annotation)
Alternative name(s):
5'-phosphoribosylglycinamide transformylaseUniRule annotation
GAR transformylaseUniRule annotation
Short name:
GARTUniRule annotation
Gene namesi
Name:purN1 PublicationUniRule annotation
Ordered Locus Names:b2500, JW2485
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10799. purN.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi70 – 701E → A: Loss of homodimerization. No effect on activity. 1 Publication
Mutagenesisi106 – 1061N → A, D, G or S: Reduces activity about 2000-fold. 1 Publication
Mutagenesisi106 – 1061N → E, H, I, K, L or Y: Loss of activity. 1 Publication
Mutagenesisi108 – 1081H → A, G, M, N, Q or R: Loss of activity. 2 Publications
Mutagenesisi108 – 1081H → E, S or T: Reduces activity about 1000-fold. 1 Publication
Mutagenesisi119 – 1191H → A: No effect. 1 Publication
Mutagenesisi121 – 1211H → Q: Increases Km for 5'-phosphoribosylglycinamide 4-fold. 1 Publication
Mutagenesisi135 – 1351S → A or L: Reduces activity about 1000-fold. 1 Publication
Mutagenesisi137 – 1371H → F or Q: No effect. 1 Publication
Mutagenesisi144 – 1441D → A, E, S or Y: Reduces activity about 1000-fold. 2 Publications
Mutagenesisi144 – 1441D → C, F, H, K, L, N, P, Q, R, T or V: Loss of activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Phosphoribosylglycinamide formyltransferasePRO_0000074943Add
BLAST

Proteomic databases

PaxDbiP08179.
PRIDEiP08179.

Expressioni

Gene expression databases

GenevestigatoriP08179.

Interactioni

Subunit structurei

Monomer. Homodimer below pH 6.8.5 Publications

Protein-protein interaction databases

IntActiP08179. 1 interaction.
STRINGi511145.b2500.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98
Helixi12 – 2211
Beta strandi25 – 3612
Helixi41 – 488
Beta strandi52 – 554
Helixi58 – 603
Beta strandi61 – 633
Helixi64 – 7512
Helixi76 – 783
Beta strandi81 – 877
Helixi94 – 996
Turni100 – 1023
Beta strandi103 – 1108
Beta strandi112 – 1143
Helixi120 – 1267
Beta strandi130 – 1389
Beta strandi141 – 1466
Beta strandi148 – 1558
Helixi162 – 18524
Beta strandi189 – 1924
Beta strandi195 – 1984

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP08179.
SMRiP08179. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08179.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 1335'-phosphoribosylglycinamide binding2 PublicationsUniRule annotation
Regioni89 – 92410-formyltetrahydrofolate binding2 PublicationsUniRule annotation
Regioni140 – 144510-formyltetrahydrofolate binding2 Publications
Regioni170 – 17345'-phosphoribosylglycinamide binding2 Publications

Sequence similaritiesi

Belongs to the GART family.CuratedUniRule annotation

Phylogenomic databases

eggNOGiCOG0299.
HOGENOMiHOG000033575.
InParanoidiP08179.
KOiK11175.
OMAiSPAFVAH.
OrthoDBiEOG615VP4.
PhylomeDBiP08179.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
HAMAPiMF_01930. PurN.
InterProiIPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR004607. PurN_trans.
[Graphical view]
PfamiPF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00639. PurN. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08179-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIVVLISGN GSNLQAIIDA CKTNKIKGTV RAVFSNKADA FGLERARQAG
60 70 80 90 100
IATHTLIASA FDSREAYDRE LIHEIDMYAP DVVVLAGFMR ILSPAFVSHY
110 120 130 140 150
AGRLLNIHPS LLPKYPGLHT HRQALENGDE EHGTSVHFVT DELDGGPVIL
160 170 180 190 200
QAKVPVFAGD SEDDITARVQ TQEHAIYPLV ISWFADGRLK MHENAAWLDG
210
QRLPPQGYAA DE
Length:212
Mass (Da):23,238
Last modified:August 1, 1988 - v1
Checksum:iD38F326BCBA103FB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13747 Genomic DNA. Translation: AAA83899.1.
U00096 Genomic DNA. Translation: AAC75553.1.
AP009048 Genomic DNA. Translation: BAA16388.1.
AF293167 Genomic DNA. Translation: AAG14584.1.
PIRiA28486. XYECGF.
RefSeqiNP_416995.1. NC_000913.3.
YP_490728.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75553; AAC75553; b2500.
BAA16388; BAA16388; BAA16388.
GeneIDi12932446.
946973.
KEGGiecj:Y75_p2453.
eco:b2500.
PATRICi32120389. VBIEscCol129921_2597.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M13747 Genomic DNA. Translation: AAA83899.1 .
U00096 Genomic DNA. Translation: AAC75553.1 .
AP009048 Genomic DNA. Translation: BAA16388.1 .
AF293167 Genomic DNA. Translation: AAG14584.1 .
PIRi A28486. XYECGF.
RefSeqi NP_416995.1. NC_000913.3.
YP_490728.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C2T X-ray 2.10 A/B 1-212 [» ]
1C3E X-ray 2.10 A/B 1-209 [» ]
1CDD X-ray 2.80 A/B 1-212 [» ]
1CDE X-ray 2.50 A/B/C/D 1-212 [» ]
1GAR X-ray 1.96 A/B 1-212 [» ]
1GRC X-ray 3.00 A/B 1-212 [» ]
1JKX X-ray 1.60 A/B/C/D 1-212 [» ]
2GAR X-ray 1.80 A 1-212 [» ]
3GAR X-ray 1.90 A 1-212 [» ]
ProteinModelPortali P08179.
SMRi P08179. Positions 1-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08179. 1 interaction.
STRINGi 511145.b2500.

Chemistry

BindingDBi P08179.

Proteomic databases

PaxDbi P08179.
PRIDEi P08179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75553 ; AAC75553 ; b2500 .
BAA16388 ; BAA16388 ; BAA16388 .
GeneIDi 12932446.
946973.
KEGGi ecj:Y75_p2453.
eco:b2500.
PATRICi 32120389. VBIEscCol129921_2597.

Organism-specific databases

EchoBASEi EB0792.
EcoGenei EG10799. purN.

Phylogenomic databases

eggNOGi COG0299.
HOGENOMi HOG000033575.
InParanoidi P08179.
KOi K11175.
OMAi SPAFVAH.
OrthoDBi EOG615VP4.
PhylomeDBi P08179.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00126 .
BioCyci EcoCyc:GART-MONOMER.
ECOL316407:JW2485-MONOMER.
MetaCyc:GART-MONOMER.
RETL1328306-WGS:GSTH-1500-MONOMER.

Miscellaneous databases

EvolutionaryTracei P08179.
PROi P08179.

Gene expression databases

Genevestigatori P08179.

Family and domain databases

Gene3Di 3.40.50.170. 1 hit.
HAMAPi MF_01930. PurN.
InterProi IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR004607. PurN_trans.
[Graphical view ]
Pfami PF00551. Formyl_trans_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53328. SSF53328. 1 hit.
TIGRFAMsi TIGR00639. PurN. 1 hit.
PROSITEi PS00373. GART. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. "Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase."
    Inglese J., Johnson D.L., Shiau A., Smith J.M., Benkovic S.J.
    Biochemistry 29:1436-1443(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  7. "N10-Formyltetrahydrofolate is the formyl donor for glycinamide ribotide transformylase in Escherichia coli."
    Dev I.K., Harvey R.J.
    J. Biol. Chem. 253:4242-4244(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "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: MUTAGENESIS OF ASP-144, PARTIAL PROTEIN SEQUENCE.
  9. "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 OF ASN-106; HIS-108; HIS-119; SER-135; HIS-137 AND ASP-144, PATHWAY.
  10. "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 OF HIS-108; HIS-121 AND ASP-144, ACTIVE SITE.
  11. "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.
  12. "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.
  13. "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.
  14. "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.

Entry informationi

Entry nameiPUR3_ECOLI
AccessioniPrimary (citable) accession number: P08179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 29, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3