Reviewed, UniProtKB/Swiss-Prot P43854 (PUR1_HAEIN)

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:	HI1207

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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.
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	Complete proteome
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	amidophosphoribosyltransferase activity Inferred from electronic annotation. Source: EC 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 505	504	Amidophosphoribosyltransferase		PRO_0000139639
Regions
	Domain	2 – 235	234	Glutamine amidotransferase type-2
Sites
	Active site	2	1	For GATase activity
	Metal binding	368	1	Magnesium By similarity
	Metal binding	369	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43854-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: CD665BB22EB88E22	FASTA	505	56,206
	10 20 30 40 50 60 MCGIVGIVSQ SPVNESIYAA LTLLQHRGQD AAGIVTVDDE NRFRLRKANG LVSDVFHQEH 70 80 90 100 110 120 MLRLQGNAGL GHVRYPTAGS SSVSEAQPFY VNSPYGVTLV HNGNLTNSVE LKEKVFKTAR 130 140 150 160 170 180 RHVNTNSDSE LLLNILANHL DHIPQDHLDP QDIFYAVRKT HKDVRGAYAC LAMIIGHGMV 190 200 210 220 230 240 AFRDPFGIRP LVLGKREENG KTDYMFASET VALDIVGFEF VRDIAAGEAV YVTFDGELYS 250 260 270 280 290 300 QQCAESAVLN PCIFEYVYFA RPDSTIDGVS VYAARVHMGE KLGQKIAKEW ADEIDNIDVV 310 320 330 340 350 360 IPVPETSTDI ALQIARVLGK PYRQGFVKNR YVGRTFIMPG QAQRISSVRR KLNTIKAEFK 370 380 390 400 410 420 DKNVLLVDDS IVRGTTSEQI VEMARSAGAK KIYFASAAPE IRYPNVYGID MPSRDELIAY 430 440 450 460 470 480 GRNVDEIAEL IGVDKLIFQD LTALTESVQL ENPAIQGFDC SVFTGEYITG DISPEYLEKI 490 500 ATQRNDNAKK KREKQASNLE IYNEQ

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22861.1.
PIR	I64189.
RefSeq	NP_439363.1.
3D structure databases
HSSP	HSSP built from PDB template 1ECB based on UniProtKB P00496.
ModBase	Search...
Genome annotation databases
GeneID	950171.
GenomeReviews	Gene locus HI1207 in contig L42023_GR.
KEGG	hin:HI1207.
NMPDR	fig|71421.1.peg.1154.
TIGR	HI1207.
Phylogenomic databases
HOGENOM	P43854.
OMA	SYCTACF.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1207-MON.
BRENDA	2.4.2.14. 109.
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...

Entry information

Entry name

PUR1_HAEIN

Accession

Primary (citable) accession number: P43854

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 74 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)