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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

Pathwayi: L-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10449. hisG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001518481 – 299ATP phosphoribosyltransferaseAdd BLAST299

Proteomic databases

EPDiP60757.
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

BioGridi4263530. 10 interactors.
IntActiP60757. 1 interactor.
STRINGi511145.b2019.

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 15Combined sources9
Helixi18 – 27Combined sources10
Beta strandi35 – 37Combined sources3
Beta strandi39 – 42Combined sources4
Beta strandi44 – 53Combined sources10
Helixi55 – 57Combined sources3
Helixi58 – 63Combined sources6
Beta strandi66 – 73Combined sources8
Helixi74 – 86Combined sources13
Beta strandi93 – 98Combined sources6
Beta strandi104 – 111Combined sources8
Helixi119 – 122Combined sources4
Beta strandi126 – 130Combined sources5
Helixi132 – 142Combined sources11
Beta strandi147 – 150Combined sources4
Helixi155 – 157Combined sources3
Helixi159 – 161Combined sources3
Beta strandi165 – 173Combined sources9
Helixi175 – 179Combined sources5
Beta strandi182 – 191Combined sources10
Beta strandi193 – 200Combined sources8
Helixi204 – 225Combined sources22
Beta strandi227 – 230Combined sources4
Turni235 – 237Combined sources3
Helixi238 – 244Combined sources7
Beta strandi265 – 271Combined sources7
Helixi275 – 283Combined sources9
Beta strandi290 – 292Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP60757.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105E21. Bacteria.
COG0040. LUCA.
HOGENOMiHOG000223247.
InParanoidiP60757.
KOiK00765.
OMAiYVMMDYD.
PhylomeDBiP60757.

Family and domain databases

Gene3Di3.30.70.120. 1 hit.
HAMAPiMF_00079. HisG_Long. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti6R → P in CAA23549 (PubMed:6170941).Curated1
Sequence conflicti49 – 50DI → GV in CAA31811 (PubMed:3062174).Curated2
Sequence conflicti263V → A in CAA31811 (PubMed:3062174).Curated1

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_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75080; AAC75080; b2019.
BAA15850; BAA15850; BAA15850.
GeneIDi946549.
KEGGiecj:JW2001.
eco: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_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4263530. 10 interactors.
IntActiP60757. 1 interactor.
STRINGi511145.b2019.

2D gel databases

SWISS-2DPAGEP60757.

Proteomic databases

EPDiP60757.
PaxDbiP60757.
PRIDEiP60757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75080; AAC75080; b2019.
BAA15850; BAA15850; BAA15850.
GeneIDi946549.
KEGGiecj:JW2001.
eco:b2019.
PATRICi32119373. VBIEscCol129921_2096.

Organism-specific databases

EchoBASEiEB0444.
EcoGeneiEG10449. hisG.

Phylogenomic databases

eggNOGiENOG4105E21. Bacteria.
COG0040. LUCA.
HOGENOMiHOG000223247.
InParanoidiP60757.
KOiK00765.
OMAiYVMMDYD.
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. 1 hit.
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...

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: November 2, 2016
This is version 120 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

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 one 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.