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P33221

- PURT_ECOLI

UniProt

P33221 - PURT_ECOLI

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Protein

Phosphoribosylglycinamide formyltransferase 2

Gene

purT

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 – 1141ATP1 PublicationUniRule annotation
Binding sitei155 – 1551ATP1 PublicationUniRule annotation
Binding sitei203 – 2031ATP1 PublicationUniRule annotation
Metal bindingi267 – 2671MagnesiumUniRule annotation
Binding sitei267 – 2671ATP1 PublicationUniRule annotation
Metal bindingi279 – 2791MagnesiumUniRule annotation
Binding sitei279 – 2791ATP1 PublicationUniRule annotation
Binding sitei286 – 28615'-phosphoribosylglycinamide
Binding sitei355 – 35515'-phosphoribosylglycinamide

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi160 – 1656ATP1 PublicationUniRule annotation
Nucleotide bindingi195 – 1984ATP1 PublicationUniRule annotation

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-UniPathway
  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-acetyllysine1 PublicationUniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP33221.
PRIDEiP33221.

Expressioni

Gene expression databases

GenevestigatoriP33221.

Interactioni

Subunit structurei

Homodimer.2 PublicationsUniRule annotation

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiWDYAQQG.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L20897 Genomic DNA. Translation: AAA23861.1 .
U00096 Genomic DNA. Translation: AAC74919.1 .
AP009048 Genomic DNA. Translation: BAA15657.1 .
PIRi A54227.
RefSeqi NP_416363.1. NC_000913.3.
YP_490111.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EYZ X-ray 1.75 A/B 1-392 [» ]
1EZ1 X-ray 1.75 A/B 1-392 [» ]
1KJ8 X-ray 1.60 A/B 2-392 [» ]
1KJ9 X-ray 1.60 A/B 2-392 [» ]
1KJI X-ray 1.60 A/B 2-392 [» ]
1KJJ X-ray 1.75 A/B 2-392 [» ]
1KJQ X-ray 1.05 A/B 2-392 [» ]
1NFE model - A 1-392 [» ]
ProteinModelPortali P33221.
SMRi P33221. Positions 2-392.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10618N.
IntActi P33221. 7 interactions.
MINTi MINT-1306001.
STRINGi 511145.b1849.

Proteomic databases

PaxDbi P33221.
PRIDEi P33221.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74919 ; AAC74919 ; b1849 .
BAA15657 ; BAA15657 ; BAA15657 .
GeneIDi 12931371.
946368.
KEGGi ecj:Y75_p1825.
eco:b1849.
PATRICi 32119019. VBIEscCol129921_1927.

Organism-specific databases

EchoBASEi EB1757.
EcoGenei EG11809. purT.

Phylogenomic databases

eggNOGi COG0027.
HOGENOMi HOG000072820.
InParanoidi P33221.
KOi K08289.
OMAi WDYAQQG.
OrthoDBi EOG6GJBVD.
PhylomeDBi P33221.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00127 .
BioCyci EcoCyc:GARTRANSFORMYL2-MONOMER.
ECOL316407:JW1838-MONOMER.
MetaCyc:GARTRANSFORMYL2-MONOMER.

Miscellaneous databases

EvolutionaryTracei P33221.
PROi P33221.

Gene expression databases

Genevestigatori P33221.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPi MF_01643. PurT.
InterProi IPR011761. 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 ]
Pfami PF02222. ATP-grasp. 1 hit.
[Graphical view ]
SUPFAMi SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsi TIGR01142. purT. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 147 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