P0AG16 (PUR1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amidophosphoribosyltransferase
Short name=ATase
EC=2.4.2.14

Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPATase

Gene names

Name:	purF
Ordered Locus Names:	b2312, JW2309

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.
Cofactor	Binds 1 magnesium ion per subunit.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Subunit structure	Homotetramer.
Sequence similarities	In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from direct assay Ref.8. Source: EcoliWiki nucleoside metabolic process Inferred from electronic annotation. Source: InterPro purine base biosynthetic process Inferred from electronic annotation. Source: InterPro purine nucleotide biosynthetic process Inferred from direct assay Ref.8. Source: EcoliWiki
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	amidophosphoribosyltransferase activity Inferred from direct assay Ref.8. Source: EcoliWiki metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 505

504

Amidophosphoribosyltransferase

PRO_0000139638

Regions

Domain

2 – 236

235

Glutamine amidotransferase type-2

Sites

Active site

2

1

For GATase activity

Metal binding

367

1

Magnesium

Metal binding

368

1

Magnesium

Experimental info

Sequence conflict

45 – 46

2

LR → SL Ref.2

Sequence conflict

45 – 46

2

LR → SL Ref.3

Sequence conflict

50

1

G → A Ref.2

Sequence conflict

50

1

G → A Ref.3

Sequence conflict

213 – 230

18

ALDTL…APGEA → GSIRWALISCVTSRRAR Ref.2

Sequence conflict

213 – 230

18

ALDTL…APGEA → GSIRWALISCVTSRRAR Ref.3

Sequence conflict

277

1

V → A Ref.2

Sequence conflict

277

1

V → A Ref.3

Sequence conflict

283

1

L → V Ref.2

Sequence conflict

283

1

L → V Ref.3

Sequence conflict

337

1

M → I in AAA24453. Ref.2

Sequence conflict

386

1

A → R in CAA30971. Ref.1

Sequence conflict

494

1

N → S Ref.2

Sequence conflict

494

1

N → S Ref.3

Secondary structure

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505

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

14 – 23

10

Helix

25 – 27

3

Beta strand

29 – 37

9

Beta strand

43 – 50

8

Helix

52 – 55

4

Helix

58 – 63

6

Beta strand

66 – 74

9

Helix

83 – 85

3

Beta strand

89 – 91

3

Beta strand

93 – 95

3

Beta strand

97 – 105

9

Helix

108 – 117

10

Helix

128 – 140

13

Beta strand

145 – 147

3

Helix

150 – 163

14

Beta strand

166 – 174

9

Turn

175 – 177

3

Beta strand

178 – 183

6

Beta strand

192 – 197

6

Beta strand

199 – 201

3

Beta strand

203 – 210

8

Helix

212 – 217

6

Beta strand

220 – 224

5

Beta strand

229 – 234

6

Beta strand

239 – 243

5

Beta strand

245 – 247

3

Helix

254 – 258

5

Helix

272 – 290

19

Beta strand

297 – 301

5

Turn

303 – 306

4

Helix

307 – 316

10

Beta strand

325 – 327

3

Helix

340 – 350

11

Beta strand

351 – 353

3

Helix

355 – 357

3

Beta strand

362 – 368

7

Beta strand

371 – 373

3

Helix

374 – 385

12

Beta strand

388 – 397

10

Beta strand

406 – 410

5

Helix

413 – 415

3

Turn

417 – 420

4

Helix

423 – 430

8

Beta strand

433 – 437

5

Helix

440 – 448

9

Helix

460 – 463

4

Helix

473 – 483

11

Helix

485 – 492

8

Helix

494 – 499

6

Sequences

	Sequence		Length	Mass (Da)
	P0AG16 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 50FD08EA85E6F2A8	FASTA	505	56,488
	10 20 30 40 50 60 MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG LVSDVFEARH 70 80 90 100 110 120 MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA HNGNLTNAHE LRKKLFEEKR 130 140 150 160 170 180 RHINTTSDSE ILLNIFASEL DNFRHYPLEA DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV 190 200 210 220 230 240 AFRDPNGIRP LVLGKRDIDE NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF 250 260 270 280 290 300 TRQCADNPVS NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI 310 320 330 340 350 360 PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK LNANRAEFRD 370 380 390 400 410 420 KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI RFPNVYGIDM PSATELIAHG 430 440 450 460 470 480 REVDEIRQII GADGLIFQDL NDLIDAVRAE NPDIQQFECS VFNGVYVTKD VDQGYLDFLD 490 500 TLRNDDAKAV QRQNEVENLE MHNEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the Escherichia coli purF gene encoding amidophosphoribosyltransferase for de novo purine nucleotide synthesis." Sampei G., Mizobuchi K. Nucleic Acids Res. 16:8717-8717(1988) [PubMed: 3047685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes." Zalkin H. Adv. Enzyme Regul. 21:225-237(1983) [PubMed: 6443594] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase." Tso J.Y., Zalkin H., van Cleemput M., Yanofsky C., Smith J.M. J. Biol. Chem. 257:3525-3531(1982) [PubMed: 6277938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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.
[6]	"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.
[7]	"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." Nonet M.L., Marvel C.C., Tolan D.R. J. Biol. Chem. 262:12209-12217(1987) [PubMed: 3040734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31 AND 483-505. Strain: K12.
[8]	"Glutamine phosphoribosylpyrophosphate amidotransferase from cloned Escherichia coli purF. NH2-terminal amino acid sequence, identification of the glutamine site, and trace metal analysis." Tso J.Y., Hermodson M.A., Zalkin H. J. Biol. Chem. 257:3532-3536(1982) [PubMed: 7037784] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24.
[9]	"Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site." Krahn J.M., Kim J.H., Burns M.R., Parry R.J., Zalkin H., Smith J.L. Biochemistry 36:11061-11068(1997) [PubMed: 9333323] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[10]	"Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli." Muchmore C.R.A., Krahn J.M., Kim J.H., Zalkin H., Smith J.L. Protein Sci. 7:39-51(1998) [PubMed: 9514258] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12423 Genomic DNA. Translation: CAA30971.1.
V00322 Genomic DNA. Translation: CAA23613.1.
M26893 Genomic DNA. Translation: AAA24453.1.
J01666 Genomic DNA. Translation: AAA24452.1.
U00096 Genomic DNA. Translation: AAC75372.1.
AP009048 Genomic DNA. Translation: BAA16158.1.
M68935, M68934 Genomic DNA. Translation: AAA23969.1. Sequence problems.

PIR

XQEC. F65003.

RefSeq

NP_416815.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ECB	X-ray	2.70	A/B/C/D	2-505	[»]
1ECC	X-ray	2.40	A/B	2-505	[»]
1ECF	X-ray	2.00	A/B	2-505	[»]
1ECG	X-ray	2.30	A/B	2-505	[»]
1ECJ	X-ray	2.50	A/B/C/D	2-505	[»]

ProteinModelPortal

P0AG16.

SMR

P0AG16. Positions 2-501.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AG16. 1 interaction.

2D gel databases

ECO2DBASE

E054.1. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002144; EBESCP00000002144; EBESCG00000001757.
EBESCT00000002145; EBESCP00000002145; EBESCG00000001757.
EBESCT00000016896; EBESCP00000016187; EBESCG00000015955.

GeneID

946794.

GenomeReviews

Gene locus JW2309 in contig AP009048_GR.
Gene locus b2312 in contig U00096_GR.

KEGG

ecj:JW2309.
eco:b2312.

PATRIC

32119995. VBIEscCol129921_2407.

Organism-specific databases

EchoBASE

EB0787.

EcoGene

EG10794. purF.

Phylogenomic databases

eggNOG

COG0034.

GeneTree

EBGT00050000009003.

OMA

SYCTACF.

PhylomeDB

P0AG16.

ProtClustDB

PRK09246.

Enzyme and pathway databases

BioCyc

EcoCyc:PRPPAMIDOTRANS-MONOMER.
MetaCyc:PRPPAMIDOTRANS-MONOMER.

Gene expression databases

Genevestigator

P0AG16.

Family and domain databases

InterPro

IPR005854. Amd_phspho_trans.
IPR000583. GATase_2.
IPR017932. GATase_II.
IPR000836. PRibTrfase.
[Graphical view]

KO

K00764.

PANTHER

PTHR11907. Amd_phspho_trans. 1 hit.

Pfam

PF00310. GATase_2. 2 hits.
PF00156. Pribosyltran. 1 hit.
[Graphical view]

PIRSF

PIRSF000485. Amd_phspho_trans. 1 hit.

TIGRFAMs

TIGR01134. PurF. 1 hit.

PROSITE

PS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

Entry information

Entry name

PUR1_ECOLI

Accession

Primary (citable) accession number: P0AG16
Secondary accession number(s): P00496 , P78092, P78191, P78192, Q47255, Q59425

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program