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P33221

- PURT_ECOLI

UniProt

P33221 - PURT_ECOLI

Protein

Phosphoribosylglycinamide formyltransferase 2

Gene

purT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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
    6. protein binding Source: IntAct

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    2. phosphorylation Source: GOC

    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.
    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.
    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

    MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM    50
    HVAHRSHVIN MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN 100
    VVPCARATKL TMNREGIRRL AAEELQLPTS TYRFADSESL FREAVADIGY 150
    PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY AQQGGRAGAG RVIVEGVVKF 200
    DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS PLALERAQEI 250
    ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF 300
    ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI 350
    RLFGKPEIDG SRRLGVALAT AESVVDAIER AKHAAGQVKV QG 392
    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.
    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.
    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

    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 1, 2014
    This is version 146 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