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P60757

- HIS1_ECOLI

UniProt

P60757 - HIS1_ECOLI

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Protein

ATP phosphoribosyltransferase

Gene
hisG, b2019, JW2001
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium Inferred.

Enzyme regulationi

Feedback inhibited by histidine. Also inhibited by AMP and PR-ATP.UniRule annotation

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
Complete GO annotation...

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299ATP phosphoribosyltransferaseUniRule annotationPRO_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.2 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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61R → P in CAA23549. 1 Publication
Sequence conflicti49 – 502DI → GV in CAA31811. 1 Publication
Sequence conflicti263 – 2631V → A in CAA31811. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 105 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

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