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P60757

- HIS1_ECOLI

UniProt

P60757 - HIS1_ECOLI

Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.1 Publication

    Catalytic activityi

    1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Feedback inhibited by histidine. Also inhibited by AMP and PR-ATP.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP phosphoribosyltransferase activity Source: EcoCyc
    3. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. histidine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Histidine biosynthesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:ATPPHOSRIBOSTRANS-MONOMER.
    ECOL316407:JW2001-MONOMER.
    MetaCyc:ATPPHOSRIBOSTRANS-MONOMER.
    UniPathwayiUPA00031; UER00006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP phosphoribosyltransferase (EC:2.4.2.17)
    Short name:
    ATP-PRT
    Short name:
    ATP-PRTase
    Gene namesi
    Name:hisG
    Ordered Locus Names:b2019, JW2001
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10449. hisG.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299ATP phosphoribosyltransferasePRO_0000151848Add
    BLAST

    Proteomic databases

    PaxDbiP60757.
    PRIDEiP60757.

    2D gel databases

    SWISS-2DPAGEP60757.

    Expressioni

    Gene expression databases

    GenevestigatoriP60757.

    Interactioni

    Subunit structurei

    Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme.3 Publications

    Protein-protein interaction databases

    IntActiP60757. 1 interaction.
    STRINGi511145.b2019.

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 159
    Helixi18 – 2710
    Beta strandi35 – 373
    Beta strandi39 – 424
    Beta strandi44 – 5310
    Helixi55 – 573
    Helixi58 – 636
    Beta strandi66 – 738
    Helixi74 – 8613
    Beta strandi93 – 986
    Beta strandi104 – 1118
    Helixi119 – 1224
    Beta strandi126 – 1305
    Helixi132 – 14211
    Beta strandi147 – 1504
    Helixi155 – 1573
    Helixi159 – 1613
    Beta strandi165 – 1739
    Helixi175 – 1795
    Beta strandi182 – 19110
    Beta strandi193 – 2008
    Helixi204 – 22522
    Beta strandi227 – 2304
    Turni235 – 2373
    Helixi238 – 2447
    Beta strandi265 – 2717
    Helixi275 – 2839
    Beta strandi290 – 2923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H3DX-ray2.70A1-299[»]
    1Q1KX-ray2.90A1-299[»]
    ProteinModelPortaliP60757.
    SMRiP60757. Positions 5-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60757.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0040.
    HOGENOMiHOG000223247.
    KOiK00765.
    OMAiTRMQGVI.
    OrthoDBiEOG66MQT3.
    PhylomeDBiP60757.

    Family and domain databases

    Gene3Di3.30.70.120. 1 hit.
    HAMAPiMF_00079. HisG_Long.
    InterProiIPR013820. ATP_PRibTrfase_cat.
    IPR018198. ATP_PRibTrfase_CS.
    IPR001348. ATP_PRibTrfase_HisG.
    IPR020621. ATP_PRibTrfase_HisG_long.
    IPR013115. HisG_C.
    IPR011322. N-reg_PII-like_a/b.
    IPR015867. N-reg_PII/ATP_PRibTrfase_C.
    [Graphical view]
    PANTHERiPTHR21403. PTHR21403. 1 hit.
    PfamiPF01634. HisG. 1 hit.
    PF08029. HisG_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF54913. SSF54913. 1 hit.
    TIGRFAMsiTIGR00070. hisG. 1 hit.
    TIGR03455. HisG_C-term. 1 hit.
    PROSITEiPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P60757-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDNTRLRIA MQKSGRLSDD SRELLARCGI KINLHTQRLI AMAENMPIDI    50
    LRVRDDDIPG LVMDGVVDLG IIGENVLEEE LLNRRAQGED PRYFTLRRLD 100
    FGGCRLSLAT PVDEAWDGPL SLNGKRIATS YPHLLKRYLD QKGISFKSCL 150
    LNGSVEVAPR AGLADAICDL VSTGATLEAN GLREVEVIYR SKACLIQRDG 200
    EMEESKQQLI DKLLTRIQGV IQARESKYIM MHAPTERLDE VIALLPGAER 250
    PTILPLAGDQ QRVAMHMVSS ETLFWETMEK LKALGASSIL VLPIEKMME 299
    Length:299
    Mass (Da):33,367
    Last modified:April 13, 2004 - v1
    Checksum:i716B2A8F4538A724
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61R → P in CAA23549. (PubMed:6170941)Curated
    Sequence conflicti49 – 502DI → GV in CAA31811. (PubMed:3062174)Curated
    Sequence conflicti263 – 2631V → A in CAA31811. (PubMed:3062174)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13462 Genomic DNA. Translation: CAA31811.1.
    X63697 Genomic DNA. Translation: CAA45224.1.
    U02070 Unassigned DNA. Translation: AAA19742.1.
    U00096 Genomic DNA. Translation: AAC75080.1.
    AP009048 Genomic DNA. Translation: BAA15850.1.
    V00284 Genomic DNA. Translation: CAA23549.1.
    PIRiB64967. XREC.
    RefSeqiNP_416523.1. NC_000913.3.
    YP_490262.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75080; AAC75080; b2019.
    BAA15850; BAA15850; BAA15850.
    GeneIDi12934536.
    946549.
    KEGGiecj:Y75_p1982.
    eco:b2019.
    PATRICi32119373. VBIEscCol129921_2096.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13462 Genomic DNA. Translation: CAA31811.1 .
    X63697 Genomic DNA. Translation: CAA45224.1 .
    U02070 Unassigned DNA. Translation: AAA19742.1 .
    U00096 Genomic DNA. Translation: AAC75080.1 .
    AP009048 Genomic DNA. Translation: BAA15850.1 .
    V00284 Genomic DNA. Translation: CAA23549.1 .
    PIRi B64967. XREC.
    RefSeqi NP_416523.1. NC_000913.3.
    YP_490262.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H3D X-ray 2.70 A 1-299 [» ]
    1Q1K X-ray 2.90 A 1-299 [» ]
    ProteinModelPortali P60757.
    SMRi P60757. Positions 5-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P60757. 1 interaction.
    STRINGi 511145.b2019.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    2D gel databases

    SWISS-2DPAGE P60757.

    Proteomic databases

    PaxDbi P60757.
    PRIDEi P60757.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75080 ; AAC75080 ; b2019 .
    BAA15850 ; BAA15850 ; BAA15850 .
    GeneIDi 12934536.
    946549.
    KEGGi ecj:Y75_p1982.
    eco:b2019.
    PATRICi 32119373. VBIEscCol129921_2096.

    Organism-specific databases

    EchoBASEi EB0444.
    EcoGenei EG10449. hisG.

    Phylogenomic databases

    eggNOGi COG0040.
    HOGENOMi HOG000223247.
    KOi K00765.
    OMAi TRMQGVI.
    OrthoDBi EOG66MQT3.
    PhylomeDBi P60757.

    Enzyme and pathway databases

    UniPathwayi UPA00031 ; UER00006 .
    BioCyci EcoCyc:ATPPHOSRIBOSTRANS-MONOMER.
    ECOL316407:JW2001-MONOMER.
    MetaCyc:ATPPHOSRIBOSTRANS-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P60757.
    PROi P60757.

    Gene expression databases

    Genevestigatori P60757.

    Family and domain databases

    Gene3Di 3.30.70.120. 1 hit.
    HAMAPi MF_00079. HisG_Long.
    InterProi IPR013820. ATP_PRibTrfase_cat.
    IPR018198. ATP_PRibTrfase_CS.
    IPR001348. ATP_PRibTrfase_HisG.
    IPR020621. ATP_PRibTrfase_HisG_long.
    IPR013115. HisG_C.
    IPR011322. N-reg_PII-like_a/b.
    IPR015867. N-reg_PII/ATP_PRibTrfase_C.
    [Graphical view ]
    PANTHERi PTHR21403. PTHR21403. 1 hit.
    Pfami PF01634. HisG. 1 hit.
    PF08029. HisG_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54913. SSF54913. 1 hit.
    TIGRFAMsi TIGR00070. hisG. 1 hit.
    TIGR03455. HisG_C-term. 1 hit.
    PROSITEi PS01316. ATP_P_PHORIBOSYLTR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."
      Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.
      J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Nucleotide sequence of the Escherichia coli K12 histidine operon revisited."
      Jovanovic G., Kostic T., Jankovic M., Savic D.J.
      J. Mol. Biol. 239:433-435(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "Identification, nucleotide sequence and expression of the regulatory region of the histidine operon of Escherichia coli K-12."
      Verde P., Frunzio R., di Nocera P.P., Blasi F., Bruni C.B.
      Nucleic Acids Res. 9:2075-2086(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    7. "Regulatory properties of phosphoribosyladenosine triphosphate synthetase. Synergism between adenosine monophosphate, phosphoribosyladenosine triphosphate, and histidine."
      Klungsoyr L., Atkinson D.E.
      Biochemistry 9:2021-2027(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, PATHWAY.
    8. "Sedimentation behaviour of phosphoribosyladenosine triphosphate synthetase. Effects of substrates and modifiers."
      Klungsoeyr L., Kryvi H.
      Biochim. Biophys. Acta 227:327-336(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. "Studies on the quaternary structure of the first enzyme for histidine biosynthesis."
      Tebar A.R., Fernandez V.M., Martin Del Rio R., Ballesteros A.O.
      Experientia 29:1477-1479(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
      Strain: K12.
    10. "Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli."
      Lohkamp B., Coggins J.R., Lapthorn A.J.
      Acta Crystallogr. D 56:1488-1491(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    11. "The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition."
      Lohkamp B., McDermott G., Campbell S.A., Coggins J.R., Lapthorn A.J.
      J. Mol. Biol. 336:131-144(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AMP AND PR-ATP, ENZYME REGULATION.

    Entry informationi

    Entry nameiHIS1_ECOLI
    AccessioniPrimary (citable) accession number: P60757
    Secondary accession number(s): P10366
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 106 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, 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