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P33221 (PURT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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 2
Short name=GART 2
EC=2.1.2.-
Alternative name(s):
5'-phosphoribosylglycinamide transformylase 2
Formate-dependent GAR transformylase
GAR transformylase 2
Gene names
Name:purT
Ordered Locus Names:b1849, JW1838
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP. HAMAP-Rule MF_01643

Catalytic activity

Formate + ATP + 5'-phospho-ribosylglycinamide = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate. HAMAP-Rule MF_01643

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 (formate route): step 1/1. HAMAP-Rule MF_01643

Subunit structure

Homodimer. Ref.6

Sequence similarities

Belongs to the PurK/PurT family.

Contains 1 ATP-grasp domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 392391Phosphoribosylglycinamide formyltransferase 2 HAMAP-Rule MF_01643
PRO_0000074956

Regions

Domain119 – 308190ATP-grasp
Nucleotide binding160 – 1656ATP HAMAP-Rule MF_01643
Nucleotide binding195 – 1984ATP HAMAP-Rule MF_01643
Region22 – 2325'-phosphoribosylglycinamide binding HAMAP-Rule MF_01643
Region362 – 36325'-phosphoribosylglycinamide binding HAMAP-Rule MF_01643

Sites

Metal binding2671Magnesium By similarity
Metal binding2791Magnesium By similarity
Binding site8215'-phosphoribosylglycinamide
Binding site1141ATP
Binding site1551ATP
Binding site2031ATP
Binding site2671ATP
Binding site2791ATP
Binding site28615'-phosphoribosylglycinamide
Binding site35515'-phosphoribosylglycinamide

Amino acid modifications

Modified residue1791N6-acetyllysine Ref.5

Secondary structure

1 ............................................................................. 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33221 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 276B3883E7403EA9

FASTA39242,434
        10         20         30         40         50         60 
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN 

        70         80         90        100        110        120 
MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN VVPCARATKL TMNREGIRRL 

       130        140        150        160        170        180 
AAEELQLPTS TYRFADSESL FREAVADIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY 

       190        200        210        220        230        240 
AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS 

       250        260        270        280        290        300 
PLALERAQEI ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF 

       310        320        330        340        350        360 
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI RLFGKPEIDG 

       370        380        390 
SRRLGVALAT AESVVDAIER AKHAAGQVKV QG

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a new purine biosynthetic enzyme: a non-folate glycinamide ribonucleotide transformylase from E. coli."
Marolewski A., Smith J.M., Benkovic S.J.
Biochemistry 33:2531-2537(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, CHARACTERIZATION.
Strain: K12.
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [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 277:1453-1474(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]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[6]"Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase."
Thoden J.B., Firestine S., Nixon A., Benkovic S.J., Holden H.M.
Biochemistry 39:8791-8802(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND BETA-FORMYL GLYCINAMIDE RIBONUCLEOTIDE, SUBUNIT.
[7]"PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site."
Thoden J.B., Firestine S.M., Benkovic S.J., Holden H.M.
J. Biol. Chem. 277:23898-23908(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH BETA-FORMYL GLYCINAMIDE RIBONUCLEOTIDE AND ATP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L20897 Genomic DNA. Translation: AAA23861.1.
U00096 Genomic DNA. Translation: AAC74919.1.
AP009048 Genomic DNA. Translation: BAA15657.1.
PIRA54227.
RefSeqNP_416363.1. NC_000913.2.
YP_490111.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EYZX-ray1.75A/B1-392[»]
1EZ1X-ray1.75A/B1-392[»]
1KJ8X-ray1.60A/B2-392[»]
1KJ9X-ray1.60A/B2-392[»]
1KJIX-ray1.60A/B2-392[»]
1KJJX-ray1.75A/B2-392[»]
1KJQX-ray1.05A/B2-392[»]
1NFEmodel-A1-392[»]
ProteinModelPortalP33221.
SMRP33221. Positions 2-392.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10618N.
IntActP33221. 7 interactions.
MINTMINT-1306001.
STRING511145.b1849.

Proteomic databases

PaxDbP33221.
PRIDEP33221.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74919; AAC74919; b1849.
BAA15657; BAA15657; BAA15657.
GeneID12931371.
946368.
KEGGecj:Y75_p1825.
eco:b1849.
PATRIC32119019. VBIEscCol129921_1927.

Organism-specific databases

EchoBASEEB1757.
EcoGeneEG11809. purT.

Phylogenomic databases

eggNOGCOG0027.
HOGENOMHOG000072820.
KOK08289.
OMAHRQEKGD.
ProtClustDBPRK09288.

Enzyme and pathway databases

BioCycEcoCyc:GARTRANSFORMYL2-MONOMER.
ECOL316407:JW1838-MONOMER.
MetaCyc:GARTRANSFORMYL2-MONOMER.
UniPathwayUPA00074; UER00127.

Gene expression databases

GenevestigatorP33221.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPMF_01643. PurT.
InterProIPR011761. ATP-grasp.
IPR003135. ATP-grasp_carboxylate-amine.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR005862. PurT.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PANTHERPTHR23047:SF2. PTHR23047:SF2. 1 hit.
PfamPF02222. ATP-grasp. 1 hit.
[Graphical view]
SUPFAMSSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.
TIGRFAMsTIGR01142. purT. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33221.

Entry information

Entry namePURT_ECOLI
AccessionPrimary (citable) accession number: P33221
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents