Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Enzyme regulationi

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

Pathway:iL-histidine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.1 Publication
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP phosphoribosyltransferase activity Source: EcoCyc
  • magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • 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.
BRENDAi2.4.2.17. 2026.
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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10449. hisG.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiP60757.
PRIDEiP60757.

2D gel databases

SWISS-2DPAGEP60757.

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 – 159Combined sources
Helixi18 – 2710Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 424Combined sources
Beta strandi44 – 5310Combined sources
Helixi55 – 573Combined sources
Helixi58 – 636Combined sources
Beta strandi66 – 738Combined sources
Helixi74 – 8613Combined sources
Beta strandi93 – 986Combined sources
Beta strandi104 – 1118Combined sources
Helixi119 – 1224Combined sources
Beta strandi126 – 1305Combined sources
Helixi132 – 14211Combined sources
Beta strandi147 – 1504Combined sources
Helixi155 – 1573Combined sources
Helixi159 – 1613Combined sources
Beta strandi165 – 1739Combined sources
Helixi175 – 1795Combined sources
Beta strandi182 – 19110Combined sources
Beta strandi193 – 2008Combined sources
Helixi204 – 22522Combined sources
Beta strandi227 – 2304Combined sources
Turni235 – 2373Combined sources
Helixi238 – 2447Combined sources
Beta strandi265 – 2717Combined sources
Helixi275 – 2839Combined sources
Beta strandi290 – 2923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP60757.
KOiK00765.
OMAiYVMMDYD.
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

        10         20         30         40         50
MTDNTRLRIA MQKSGRLSDD SRELLARCGI KINLHTQRLI AMAENMPIDI
60 70 80 90 100
LRVRDDDIPG LVMDGVVDLG IIGENVLEEE LLNRRAQGED PRYFTLRRLD
110 120 130 140 150
FGGCRLSLAT PVDEAWDGPL SLNGKRIATS YPHLLKRYLD QKGISFKSCL
160 170 180 190 200
LNGSVEVAPR AGLADAICDL VSTGATLEAN GLREVEVIYR SKACLIQRDG
210 220 230 240 250
EMEESKQQLI DKLLTRIQGV IQARESKYIM MHAPTERLDE VIALLPGAER
260 270 280 290
PTILPLAGDQ QRVAMHMVSS ETLFWETMEK LKALGASSIL VLPIEKMME
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:
EMBLi
GenBanki
DDBJi
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.
WP_000131782.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75080; AAC75080; b2019.
BAA15850; BAA15850; BAA15850.
GeneIDi946549.
KEGGieco:b2019.
PATRICi32119373. VBIEscCol129921_2096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000131782.1. NZ_CP010445.1.

3D structure databases

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

Protein-protein interaction databases

IntActiP60757. 1 interaction.
STRINGi511145.b2019.

2D gel databases

SWISS-2DPAGEP60757.

Proteomic databases

PaxDbiP60757.
PRIDEiP60757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75080; AAC75080; b2019.
BAA15850; BAA15850; BAA15850.
GeneIDi946549.
KEGGieco:b2019.
PATRICi32119373. VBIEscCol129921_2096.

Organism-specific databases

EchoBASEiEB0444.
EcoGeneiEG10449. hisG.

Phylogenomic databases

eggNOGiCOG0040.
HOGENOMiHOG000223247.
InParanoidiP60757.
KOiK00765.
OMAiYVMMDYD.
OrthoDBiEOG66MQT3.
PhylomeDBiP60757.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.
BioCyciEcoCyc:ATPPHOSRIBOSTRANS-MONOMER.
ECOL316407:JW2001-MONOMER.
MetaCyc:ATPPHOSRIBOSTRANS-MONOMER.
BRENDAi2.4.2.17. 2026.

Miscellaneous databases

EvolutionaryTraceiP60757.
PROiP60757.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 113 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

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.