Reviewed, UniProtKB/Swiss-Prot P00497 (PUR1_BACSU)

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:	BSU06490

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	476 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. Binds 1 4Fe-4S cluster per subunit. The 4Fe-4S cluster requires a potential lower than -600 mV for reduction.
Enzyme regulation	Allosterically regulated; subject to end product regulation by purine nucleotides.
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	4Fe-4S Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW 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 electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium 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

Propeptide

1 – 11

11

PRO_0000029251

Chain

12 – 476

465

Amidophosphoribosyltransferase

PRO_0000029252

Regions

Domain

12 – 231

220

Glutamine amidotransferase type-2

Sites

Active site

12

1

For GATase activity Ref.5

Metal binding

247

1

Iron-sulfur (4Fe-4S)

Metal binding

294

1

Magnesium

Metal binding

356

1

Magnesium

Metal binding

357

1

Magnesium

Metal binding

393

1

Iron-sulfur (4Fe-4S)

Metal binding

448

1

Iron-sulfur (4Fe-4S)

Metal binding

451

1

Iron-sulfur (4Fe-4S)

Experimental info

Mutagenesis

12

1

C → F: Loss of enzyme activity and N-terminal processing. Ref.6

Mutagenesis

394

1

F → V: Partial loss of activity.

Mutagenesis

442

1

D → S: Partial loss of activity.

Mutagenesis

448

1

C → S: Loss of activity.

Mutagenesis

451

1

C → S: Loss of activity.

Mutagenesis

452

1

F → C: Lethal.

Sequence conflict

413

1

E → G Ref.1

Sequence conflict

413

1

E → G in AAA22680. Ref.2

Secondary structure

1

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476

Helix Strand Turn

Details...

Beta strand

13 – 19

7

Helix

23 – 33

11

Helix

34 – 37

4

Beta strand

40 – 47

8

Beta strand

52 – 59

8

Helix

61 – 64

4

Turn

70 – 72

3

Beta strand

75 – 83

9

Helix

92 – 94

3

Beta strand

95 – 101

7

Turn

103 – 105

3

Beta strand

108 – 116

9

Helix

119 – 128

10

Helix

138 – 147

10

Helix

154 – 162

9

Beta strand

167 – 174

8

Beta strand

176 – 183

8

Beta strand

192 – 196

5

Beta strand

199 – 205

7

Helix

207 – 212

6

Beta strand

215 – 219

5

Beta strand

224 – 229

6

Beta strand

232 – 238

7

Helix

248 – 252

5

Helix

266 – 281

16

Beta strand

286 – 289

4

Turn

292 – 295

4

Helix

296 – 306

11

Beta strand

314 – 316

3

Helix

329 – 334

6

Beta strand

338 – 342

5

Helix

344 – 347

4

Beta strand

351 – 357

7

Beta strand

360 – 362

3

Helix

363 – 374

12

Beta strand

378 – 386

9

Turn

397 – 399

3

Turn

407 – 409

3

Helix

412 – 419

8

Beta strand

422 – 426

5

Helix

429 – 436

8

Turn

443 – 446

4

Helix

450 – 453

4

Helix

467 – 469

3

Sequences

	Sequence		Length	Mass (Da)
	P00497-1 [UniParc]. Last modified July 7, 2009. Version 2. Checksum: 6BC2FDA3288002F0	FASTA	476	51,692
	10 20 30 40 50 60 MLAEIKGLNE ECGVFGIWGH EEAPQITYYG LHSLQHRGQE GAGIVATDGE KLTAHKGQGL 70 80 90 100 110 120 ITEVFQNGEL SKVKGKGAIG HVRYATAGGG GYENVQPLLF RSQNNGSLAL AHNGNLVNAT 130 140 150 160 170 180 QLKQQLENQG SIFQTSSDTE VLAHLIKRSG HFTLKDQIKN SLSMLKGAYA FLIMTETEMI 190 200 210 220 230 240 VALDPNGLRP LSIGMMGDAY VVASETCAFD VVGATYLREV EPGEMLIIND EGMKSERFSM 250 260 270 280 290 300 NINRSICSME YIYFSRPDSN IDGINVHSAR KNLGKMLAQE SAVEADVVTG VPDSSISAAI 310 320 330 340 350 360 GYAEATGIPY ELGLIKNRYV GRTFIQPSQA LREQGVRMKL SAVRGVVEGK RVVMVDDSIV 370 380 390 400 410 420 RGTTSRRIVT MLREAGATEV HVKISSPPIA HPCFYGIDTS THEELIASSH SVEEIRQEIG 430 440 450 460 470 ADTLSFLSVE GLLKGIGRKY DDSNCGQCLA CFTGKYPTEI YQDTVLPHVK EAVLTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase gene in Escherichia coli. Nucleotide sequence determination and properties of the plasmid-encoded enzyme." Makaroff C.A., Zalkin H., Switzer R.L., Vollmer S.J. J. Biol. Chem. 258:10586-10593(1983) [PubMed: 6411717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis." Ebbole D.J., Zalkin H. J. Biol. Chem. 262:8274-8287(1987) [PubMed: 3036807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 413.
[5]	"The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase." Vollmer S.J., Switzer R.L., Hermodson M.A., Bower S.G., Zalkin H. J. Biol. Chem. 258:10582-10585(1983) [PubMed: 6411716] [Abstract] Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 12-35.
[6]	"Glutamine amidotransferase function. Replacement of the active-site cysteine in glutamine phosphoribosylpyrophosphate amidotransferase by site-directed mutagenesis." Maentsaelae P., Zalkin H. J. Biol. Chem. 259:14230-14236(1984) [PubMed: 6094545] [Abstract] Cited for: MUTAGENESIS OF CYS-12.
[7]	"Mutagenesis of ligands to the [4 Fe-4S] center of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase." Makaroff C.A., Paluh J.L., Zalkin H. J. Biol. Chem. 261:11416-11423(1986) [PubMed: 3090047] [Abstract] Cited for: MUTAGENESIS.
[8]	"Structure of the allosteric regulatory enzyme of purine biosynthesis." Smith J.L., Zaluzec E.J., Wery J.-P., Niu L., Switzer R.L., Zalkin H., Satow Y. Science 264:1427-1433(1994) [PubMed: 8197456] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[9]	"Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides." Chen S., Tomchick D.R., Wolle D., Hu P., Smith J.L., Switzer R.L., Zalkin H. Biochemistry 36:10718-10726(1997) [PubMed: 9271502] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02732 Genomic DNA. Translation: AAA22680.1.
AL009126 Genomic DNA. Translation: CAB12469.2.

PIR

XQBS. A00582.

RefSeq

NP_388531.2.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AO0	X-ray	2.80	A/B/C/D	12-470	[»]
1GPH	X-ray	3.00	1/2/3/4	12-476	[»]

ModBase

Search...

Protein family/group databases

MEROPS

C44.001.

Genome annotation databases

GeneID

936046.

GenomeReviews

Gene locus BSU06490 in contig AL009126_GR.

KEGG

bsu:BSU06490.

NMPDR

fig|224308.1.peg.650.

Organism-specific databases

SubtiList

BG10707. purF. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P00497.

OMA

GIPFELG.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU0650-MON.

BRENDA

2.4.2.14. 150.

Family and domain databases

InterPro

IPR005854. Amd_phspho_trans.
IPR000583. GATase_2.
IPR017932. GATase_II.
IPR002375. Pr/py_Pribosyl_transf_CS.
IPR000836. PRibTrfase.
[Graphical view]

PANTHER

PTHR11907. Amd_phspho_trans. 1 hit.

Pfam

PF00310. GATase_2. 1 hit.
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 Resources

DrugBank

DB00131. Adenosine monophosphate.

Entry information

Entry name

PUR1_BACSU

Accession

Primary (citable) accession number: P00497

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 7, 2009
Last modified:	November 3, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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