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Protein

ATP phosphoribosyltransferase

Gene

hisG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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: InterPro

GO - Biological processi

  • histidine biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ATPPHOSRIBOSTRANS-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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB01661 Phosphoribosyl Atp

PTM / Processingi

Molecule processing

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

Proteomic databases

EPDiP60757
PaxDbiP60757
PRIDEiP60757

2D gel databases

SWISS-2DPAGEiP60757

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

BioGridi426353024 interactors.
IntActiP60757 1 interactor.
STRINGi316385.ECDH10B_2167

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

Gene3Di3.30.70.1201 hit
HAMAPiMF_00079 HisG_Long, 1 hit
InterProiView protein in InterPro
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
PANTHERiPTHR21403 PTHR21403, 1 hit
PfamiView protein in Pfam
PF01634 HisG, 1 hit
PF08029 HisG_C, 1 hit
SUPFAMiSSF54913 SSF54913, 1 hit
TIGRFAMsiTIGR00070 hisG, 1 hit
TIGR03455 HisG_C-term, 1 hit
PROSITEiView protein in PROSITE
PS01316 ATP_P_PHORIBOSYLTR, 1 hit

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
PATRICifig|1411691.4.peg.233

Similar proteinsi

Entry informationi

Entry nameiHIS1_ECOLI
AccessioniPrimary (citable) accession number: P60757
Secondary accession number(s): P10366
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: March 28, 2018
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome