ATP phosphoribosyltransferase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P60757 (HIS1_ECOLI)

Last modified February 9, 2010. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    ATP phosphoribosyltransferase
      Short name=ATP-PRTase
      Short name=ATP-PRT
    EC=2.4.2.17

Gene names

Name:	hisG
Ordered Locus Names:	b2019, JW2001

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

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 MF_00079
Catalytic activity	1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00079
Cofactor	Magnesium Probable. HAMAP MF_00079
Enzyme regulation	Feedback inhibited by histidine. Also inhibited by AMP and PR-ATP. HAMAP MF_00079
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP 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 MF_00079.
Sequence similarities	Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Hide | Top

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP phosphoribosyltransferase activity Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

ATP phosphoribosyltransferase HAMAP MF_00079

PRO_0000151848

Experimental info

Sequence conflict

R → P in CAA23549. Ref.6

Sequence conflict

49 – 50

DI → GV in CAA31811. Ref.1

Sequence conflict

263

V → A in CAA31811. Ref.1

Secondary structure

299

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P60757-1 [UniParc].

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

FASTA

299

33,367

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 3062174] [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: 8201624] [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. Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 6170941] [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: 4927808] [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: 4358959] [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: 11185885] [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: 14741209] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AMP AND PR-ATP.

Hide | Top

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.

PIR

XREC. B64967.

RefSeq

AP_002620.1.
NP_416523.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H3D	X-ray	2.70	A	1-299	[»]
1Q1K	X-ray	2.90	A	1-299	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P60757.

2-D gel databases

SWISS-2DPAGE

P60757.

Genome annotation databases

GeneID

946549.

GenomeReviews

Gene locus JW2001 in contig AP009048_GR.
Gene locus b2019 in contig U00096_GR.

KEGG

ecj:JW2001.
eco:b2019.

Organism-specific databases

EchoBASE

EB0444.

EcoGene

EG10449. hisG.

CMR

Search...

Phylogenomic databases

eggNOG

COG0040.

HOGENOM

HBG391868.

OMA

YLRPRDI.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPPHOSRIBOSTRANS-MONOMER.
ECOL168927:B2019-MONOMER.
MetaCyc:ATPPHOSRIBOSTRANS-MONOMER.

Gene expression databases

Genevestigator

P60757.

Family and domain databases

HAMAP

MF_00079. HisG_Long.
[Tree]

InterPro

IPR001348. ATP_PRibTrfase.
IPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR020621. ATP_PRibTrfase_subgr.
IPR013115. HisG_C.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
[Graphical view]

Gene3D

G3DSA:3.30.70.120. PII_glnB. 1 hit.

PANTHER

PTHR21403. ATP_phspho_trans. 1 hit.

Pfam

PF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.

PROSITE

PS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

Hide | Top

Entry information

Entry name

HIS1_ECOLI

Accession

Primary (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:	February 9, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top