Reviewed, UniProtKB/Swiss-Prot O26742 (PUR1_METTH)

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:	MTH_646

Organism

Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	474 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 By similarity. Binds 1 4Fe-4S cluster per subunit By similarity.
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	4Fe-4S Iron Iron-sulfur 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	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 – 10	10	By similarity		PRO_0000029275
	Chain	11 – 474	464	Amidophosphoribosyltransferase		PRO_0000029276
Regions
	Domain	11 – 234	224	Glutamine amidotransferase type-2
Sites
	Active site	11	1	For GATase activity By similarity
	Metal binding	250	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	297	1	Magnesium By similarity
	Metal binding	359	1	Magnesium By similarity
	Metal binding	360	1	Magnesium By similarity
	Metal binding	396	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	447	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	450	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O26742-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 16BAF93BBF15A0D2	FASTA	474	52,660
	10 20 30 40 50 60 MLGESEVRDK CGIVGIYSQD KKTGVASQIY YALYALQHRG QESAGISTFN GNDILTHRGM 70 80 90 100 110 120 GLVCDVFNPE KLEELKGNVG IGHVRYSTTG ESRIENSQPF WSEFQGGKIA IAHNGDIINS 130 140 150 160 170 180 MELREELEEE GHNFVSTTDS EVICHLLSRE YDEKPNMIYS IKRVSEQLVG SYSLVVLLNQ 190 200 210 220 230 240 DLYVVRDPVG IKPLAFARKG STQIVASETV AFDVIGAEHV RDVQPGEILH LNRGKSYWVA 250 260 270 280 290 300 NAPNTRRAHC MFEYVYFARP DSVIDGRNVY RVRLNIGEAL YREHPANADV VVPVPDSSIP 310 320 330 340 350 360 AAIGYSRASG IPYGEGLIKN RYVGRTFIMP TQEERETAVK LKMNPIRSEL EGKRIVLIDD 370 380 390 400 410 420 SIVRGTTSRA LIDIIRDAGA EEIHLRIGCP PIKSPCYYGI AMATKKELIA STRNVEEIRR 430 440 450 460 470 IIGVDSLGYL SIESLVECIG IKKGFLCTGC LDGDYPTPLP SDISEYEAMR SCSR

References

[1]

"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000666 Genomic DNA. Translation: AAB85151.1.
PIR	H69185.
RefSeq	NP_275788.1.
3D structure databases
HSSP	HSSP built from PDB template 1AO0 based on UniProtKB P00497.
ModBase	Search...
Protein-protein interaction databases
STRING	O26742.
Protein family/group databases
MEROPS	C44.001.
Genome annotation databases
GeneID	1470607.
GenomeReviews	Gene locus MTH_646 in contig AE000666_GR.
KEGG	mth:MTH646.
NMPDR	fig|187420.1.peg.643.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O26742.
OMA	GIPFELG.
Enzyme and pathway databases
BioCyc	MTHE187420:MTH646-MON.
BRENDA	2.4.2.14. 270.
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_METTH

Accession

Primary (citable) accession number: O26742

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 76 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)