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Protein

Phosphoribosylglycinamide formyltransferase 2

Gene

purT

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

Functioni

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.

Catalytic activityi

Formate + ATP + 5'-phospho-ribosylglycinamide = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 8215'-phosphoribosylglycinamide
Binding sitei114 – 1141ATPUniRule annotation1 Publication
Binding sitei155 – 1551ATPUniRule annotation1 Publication
Binding sitei203 – 2031ATPUniRule annotation1 Publication
Metal bindingi267 – 2671MagnesiumUniRule annotation
Binding sitei267 – 2671ATPUniRule annotation1 Publication
Metal bindingi279 – 2791MagnesiumUniRule annotation
Binding sitei279 – 2791ATPUniRule annotation1 Publication
Binding sitei286 – 28615'-phosphoribosylglycinamide
Binding sitei355 – 35515'-phosphoribosylglycinamide

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi160 – 1656ATPUniRule annotation1 Publication
Nucleotide bindingi195 – 1984ATPUniRule annotation1 Publication

GO - Molecular functioni

  1. acetate kinase activity Source: EcoCyc
  2. ATP binding Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: InterPro
  4. phosphoribosylglycinamide formyltransferase 2 activity Source: UniProtKB-HAMAP
  5. phosphoribosylglycinamide formyltransferase activity Source: InterPro

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
  2. phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GARTRANSFORMYL2-MONOMER.
ECOL316407:JW1838-MONOMER.
MetaCyc:GARTRANSFORMYL2-MONOMER.
UniPathwayiUPA00074; UER00127.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylglycinamide formyltransferase 2UniRule annotation (EC:2.1.2.-UniRule annotation)
Short name:
GART 2UniRule annotation
Alternative name(s):
5'-phosphoribosylglycinamide transformylase 2UniRule annotation
Formate-dependent GAR transformylaseUniRule annotation
GAR transformylase 2UniRule annotation
Gene namesi
Name:purTUniRule annotation
Ordered Locus Names:b1849, JW1838
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11809. purT.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 392391Phosphoribosylglycinamide formyltransferase 2PRO_0000074956Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791N6-acetyllysineUniRule annotation1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP33221.
PRIDEiP33221.

Expressioni

Gene expression databases

GenevestigatoriP33221.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ispAP229393EBI-553029,EBI-553011

Protein-protein interaction databases

DIPiDIP-10618N.
IntActiP33221. 7 interactions.
MINTiMINT-1306001.
STRINGi511145.b1849.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Helixi22 – 3211Combined sources
Turni33 – 353Combined sources
Beta strandi37 – 448Combined sources
Helixi48 – 525Combined sources
Beta strandi53 – 586Combined sources
Helixi64 – 7411Combined sources
Beta strandi77 – 815Combined sources
Helixi88 – 969Combined sources
Beta strandi100 – 1034Combined sources
Helixi105 – 1128Combined sources
Helixi114 – 1229Combined sources
Beta strandi132 – 1376Combined sources
Helixi138 – 14811Combined sources
Beta strandi150 – 1578Combined sources
Turni161 – 1644Combined sources
Beta strandi166 – 1683Combined sources
Helixi171 – 1733Combined sources
Helixi174 – 18411Combined sources
Helixi186 – 1883Combined sources
Beta strandi192 – 1965Combined sources
Beta strandi201 – 21111Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi229 – 2357Combined sources
Helixi241 – 25818Combined sources
Beta strandi260 – 27112Combined sources
Beta strandi274 – 28310Combined sources
Helixi286 – 2905Combined sources
Helixi291 – 2944Combined sources
Beta strandi295 – 2973Combined sources
Helixi299 – 3079Combined sources
Beta strandi319 – 3268Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi336 – 3383Combined sources
Helixi340 – 3423Combined sources
Beta strandi348 – 3525Combined sources
Beta strandi358 – 3614Combined sources
Beta strandi365 – 3706Combined sources
Helixi374 – 38714Combined sources
Beta strandi389 – 3913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP33221.
SMRiP33221. Positions 2-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33221.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 308190ATP-graspUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 2325'-phosphoribosylglycinamide binding
Regioni362 – 36325'-phosphoribosylglycinamide binding

Sequence similaritiesi

Belongs to the PurK/PurT family.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0027.
HOGENOMiHOG000072820.
InParanoidiP33221.
KOiK08289.
OMAiIFGVEFF.
OrthoDBiEOG6GJBVD.
PhylomeDBiP33221.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_01643. PurT.
InterProiIPR011761. 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]
PfamiPF02222. ATP-grasp. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01142. purT. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33221-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM
60 70 80 90 100
HVAHRSHVIN MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN
110 120 130 140 150
VVPCARATKL TMNREGIRRL AAEELQLPTS TYRFADSESL FREAVADIGY
160 170 180 190 200
PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY AQQGGRAGAG RVIVEGVVKF
210 220 230 240 250
DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS PLALERAQEI
260 270 280 290 300
ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
310 320 330 340 350
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI
360 370 380 390
RLFGKPEIDG SRRLGVALAT AESVVDAIER AKHAAGQVKV QG
Length:392
Mass (Da):42,434
Last modified:January 23, 2007 - v3
Checksum:i276B3883E7403EA9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20897 Genomic DNA. Translation: AAA23861.1.
U00096 Genomic DNA. Translation: AAC74919.1.
AP009048 Genomic DNA. Translation: BAA15657.1.
PIRiA54227.
RefSeqiNP_416363.1. NC_000913.3.
YP_490111.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74919; AAC74919; b1849.
BAA15657; BAA15657; BAA15657.
GeneIDi12931371.
946368.
KEGGiecj:Y75_p1825.
eco:b1849.
PATRICi32119019. VBIEscCol129921_1927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20897 Genomic DNA. Translation: AAA23861.1.
U00096 Genomic DNA. Translation: AAC74919.1.
AP009048 Genomic DNA. Translation: BAA15657.1.
PIRiA54227.
RefSeqiNP_416363.1. NC_000913.3.
YP_490111.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP33221.
SMRiP33221. Positions 2-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10618N.
IntActiP33221. 7 interactions.
MINTiMINT-1306001.
STRINGi511145.b1849.

Proteomic databases

PaxDbiP33221.
PRIDEiP33221.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74919; AAC74919; b1849.
BAA15657; BAA15657; BAA15657.
GeneIDi12931371.
946368.
KEGGiecj:Y75_p1825.
eco:b1849.
PATRICi32119019. VBIEscCol129921_1927.

Organism-specific databases

EchoBASEiEB1757.
EcoGeneiEG11809. purT.

Phylogenomic databases

eggNOGiCOG0027.
HOGENOMiHOG000072820.
InParanoidiP33221.
KOiK08289.
OMAiIFGVEFF.
OrthoDBiEOG6GJBVD.
PhylomeDBiP33221.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00127.
BioCyciEcoCyc:GARTRANSFORMYL2-MONOMER.
ECOL316407:JW1838-MONOMER.
MetaCyc:GARTRANSFORMYL2-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP33221.
PROiP33221.

Gene expression databases

GenevestigatoriP33221.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPiMF_01643. PurT.
InterProiIPR011761. 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]
PfamiPF02222. ATP-grasp. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01142. purT. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. "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, IDENTIFICATION BY 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.

Entry informationi

Entry nameiPURT_ECOLI
AccessioniPrimary (citable) accession number: P33221
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 149 of the entry and version 3 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.