P60757 (HIS1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Evidence 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-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.

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 Reference proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from direct assay PubMed 165751. Source: EcoCyc
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 PubMed 165751. Source: EcoCyc magnesium ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 299

299

ATP phosphoribosyltransferase HAMAP-Rule MF_00079

PRO_0000151848

Experimental info

Sequence conflict

6

1

R → P in CAA23549. Ref.6

Sequence conflict

49 – 50

2

DI → GV in CAA31811. Ref.1

Sequence conflict

263

1

V → A in CAA31811. Ref.1

Secondary structure

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299

Helix Strand Turn

Details...

Beta strand

7 – 15

9

Helix

18 – 27

10

Beta strand

35 – 37

3

Beta strand

39 – 42

4

Beta strand

44 – 53

10

Helix

55 – 57

3

Helix

58 – 63

6

Beta strand

66 – 73

8

Helix

74 – 86

13

Beta strand

93 – 98

6

Beta strand

104 – 111

8

Helix

119 – 122

4

Beta strand

126 – 130

5

Helix

132 – 142

11

Beta strand

147 – 150

4

Helix

155 – 157

3

Helix

159 – 161

3

Beta strand

165 – 173

9

Helix

175 – 179

5

Beta strand

182 – 191

10

Beta strand

193 – 200

8

Helix

204 – 225

22

Beta strand

227 – 230

4

Turn

235 – 237

3

Helix

238 – 244

7

Beta strand

265 – 271

7

Helix

275 – 283

9

Beta strand

290 – 292

3

Sequences

	Sequence		Length	Mass (Da)
	P60757 [UniParc]. Last modified April 13, 2004. Version 1. Checksum: 716B2A8F4538A724	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

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] [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. , 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 277:1453-1474(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.

PIR

XREC. B64967.

RefSeq

NP_416523.1. NC_000913.2.
YP_490262.1. NC_007779.1.

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	[»]

ProteinModelPortal

P60757.

SMR

P60757. Positions 5-299.

ModBase

Search...

Protein-protein interaction databases

IntAct

P60757. 1 interaction.

STRING

511145.b2019.

2D gel databases

SWISS-2DPAGE

P60757.

Proteomic databases

PaxDb

P60757.

PRIDE

P60757.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75080; AAC75080; b2019.
BAA15850; BAA15850; BAA15850.

GeneID

12934536.
946549.

KEGG

ecj:Y75_p1982.
eco:b2019.

PATRIC

32119373. VBIEscCol129921_2096.

Organism-specific databases

EchoBASE

EB0444.

EcoGene

EG10449. hisG.

Phylogenomic databases

eggNOG

COG0040.

HOGENOM

HOG000223247.

KO

K00765.

OMA

VATEFPN.

ProtClustDB

PRK00489.

Enzyme and pathway databases

BioCyc

EcoCyc:ATPPHOSRIBOSTRANS-MONOMER.
ECOL316407:JW2001-MONOMER.
MetaCyc:ATPPHOSRIBOSTRANS-MONOMER.

UniPathway

UPA00031; UER00006.

Gene expression databases

Genevestigator

P60757.

Family and domain databases

Gene3D

3.30.70.120. 1 hit.

HAMAP

MF_00079. HisG_Long.

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.
[Graphical view]

PANTHER

PTHR21403. PTHR21403. 1 hit.

Pfam

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

SUPFAM

SSF54913. N-reg_PII-like_a/b. 1 hit.

TIGRFAMs

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

PROSITE

PS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P60757.

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:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program