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P60757 (HIS1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP phosphoribosyltransferase

Short name=ATP-PRT
Short name=ATP-PRTase
EC=2.4.2.17
Gene names
Name:hisG
Ordered Locus Names:b2019, JW2001
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00079

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00079

Cofactor

Magnesium Probable.

Enzyme regulation

Feedback inhibited by histidine. Also inhibited by AMP and PR-ATP. HAMAP-Rule MF_00079

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP-Rule MF_00079

Subunit structure

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. Ref.7 Ref.8

Subcellular location

Cytoplasm HAMAP-Rule MF_00079.

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_0000151848

Experimental info

Sequence conflict61R → P in CAA23549. Ref.6
Sequence conflict49 – 502DI → GV in CAA31811. Ref.1
Sequence conflict2631V → A in CAA31811. Ref.1

Secondary structure

...................................................... 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60757 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: 716B2A8F4538A724

FASTA29933,367
        10         20         30         40         50         60 
MTDNTRLRIA MQKSGRLSDD SRELLARCGI KINLHTQRLI AMAENMPIDI LRVRDDDIPG 

        70         80         90        100        110        120 
LVMDGVVDLG IIGENVLEEE LLNRRAQGED PRYFTLRRLD FGGCRLSLAT PVDEAWDGPL 

       130        140        150        160        170        180 
SLNGKRIATS YPHLLKRYLD QKGISFKSCL LNGSVEVAPR AGLADAICDL VSTGATLEAN 

       190        200        210        220        230        240 
GLREVEVIYR SKACLIQRDG EMEESKQQLI DKLLTRIQGV IQARESKYIM MHAPTERLDE 

       250        260        270        280        290 
VIALLPGAER PTILPLAGDQ QRVAMHMVSS ETLFWETMEK LKALGASSIL VLPIEKMME 

« Hide

References

« Hide 'large scale' references
[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]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"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.
[8]"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.
[9]"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.
[10]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRXREC. B64967.
RefSeqNP_416523.1. NC_000913.3.
YP_490262.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3DX-ray2.70A1-299[»]
1Q1KX-ray2.90A1-299[»]
ProteinModelPortalP60757.
SMRP60757. Positions 5-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP60757. 1 interaction.
STRING511145.b2019.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

2D gel databases

SWISS-2DPAGEP60757.

Proteomic databases

PaxDbP60757.
PRIDEP60757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75080; AAC75080; b2019.
BAA15850; BAA15850; BAA15850.
GeneID12934536.
946549.
KEGGecj:Y75_p1982.
eco:b2019.
PATRIC32119373. VBIEscCol129921_2096.

Organism-specific databases

EchoBASEEB0444.
EcoGeneEG10449. hisG.

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223247.
KOK00765.
OMAVATEFPN.
OrthoDBEOG66MQT3.
PhylomeDBP60757.
ProtClustDBPRK00489.

Enzyme and pathway databases

BioCycEcoCyc:ATPPHOSRIBOSTRANS-MONOMER.
ECOL316407:JW2001-MONOMER.
MetaCyc:ATPPHOSRIBOSTRANS-MONOMER.
UniPathwayUPA00031; UER00006.

Gene expression databases

GenevestigatorP60757.

Family and domain databases

Gene3D3.30.70.120. 1 hit.
HAMAPMF_00079. HisG_Long.
InterProIPR013820. 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]
PANTHERPTHR21403. PTHR21403. 1 hit.
PfamPF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]
SUPFAMSSF54913. SSF54913. 1 hit.
TIGRFAMsTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60757.
PROP60757.

Entry information

Entry nameHIS1_ECOLI
AccessionPrimary (citable) accession number: P60757
Secondary accession number(s): P10366
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene