purF

Functionⁱ

Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.UniRule annotation

Catalytic activityⁱ

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H₂O.UniRule annotation

Cofactorⁱ

Protein has several cofactor binding sites:

Mg²⁺
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_01931
Note: Binds 1 Mg²⁺ ion per subunit.
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_01931
[4Fe-4S] cluster
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_01931
- PIRSR:PIRSR000485-3
Note: Binds 1 [4Fe-4S] cluster per subunit.
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_01931
- PIRSR:PIRSR000485-3

Pathwayⁱ: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

Amidophosphoribosyltransferase (purF)
Phosphoribosylamine--glycine ligase (purD)

This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	33	For GATase activityUniRule annotation	1
Active siteⁱ	33	NucleophileUniRule annotation	1
Metal bindingⁱ	267	Iron-sulfur (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	314	MagnesiumUniRule annotation	1
Metal bindingⁱ	376	MagnesiumUniRule annotation	1
Metal bindingⁱ	377	MagnesiumUniRule annotation	1
Metal bindingⁱ	413	Iron-sulfur (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	469	Iron-sulfur (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	472	Iron-sulfur (4Fe-4S)UniRule annotation	1

GO - Molecular functionⁱ

4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
amidophosphoribosyltransferase activity Source: UniProtKB-UniRule
magnesium ion binding Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

'de novo' IMP biosynthetic process Source: UniProtKB-UniRule
glutamine metabolic process Source: UniProtKB-KW
nucleoside metabolic process Source: InterPro
purine nucleobase biosynthetic process Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	GlycosyltransferaseUniRule annotationImported, Transferase
Biological process	Purine biosynthesisUniRule annotation
Ligand	4Fe-4SUniRule annotation, Iron, Iron-sulfur, MagnesiumUniRule annotation, Metal-binding

Enzyme and pathway databases

BioCycⁱ	PPOL886882:G1GOE-865-MONOMER.
UniPathwayⁱ	UPA00074; UER00124.

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	C44.001.

MEROPSⁱ

C44.001.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: AmidophosphoribosyltransferaseUniRule annotation (EC:2.4.2.14UniRule annotation) Short name: ATaseUniRule annotation Alternative name(s): Glutamine phosphoribosylpyrophosphate amidotransferaseUniRule annotation Short name: GPATaseUniRule annotation
Gene namesⁱ	Name:purFUniRule annotationImported ORF Names:PPSC2_04245Imported
Organismⁱ	Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa)Imported
Taxonomic identifierⁱ	886882 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus › Paenibacillus polymyxa
Proteomesⁱ	UP000006868 Componentⁱ: Chromosome

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	886882.PPSC2_c0858.

STRINGⁱ

886882.PPSC2_c0858.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	E3ECX2.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	33 – 250	Glutamine amidotransferase type-2InterPro annotationAdd BLAST		218

Sequence similaritiesⁱ

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.UniRule annotation

Keywords - Domainⁱ

Glutamine amidotransferaseUniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105CBA. Bacteria. COG0034. LUCA.
HOGENOMⁱ	HOG000033688.
KEGG Orthology (KO) More...KOⁱ	K00764.
OMAⁱ	FRPLCLG.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H0061.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00715. GPATase_N. 1 hit. cd06223. PRTases_typeI. 1 hit.
Gene3Dⁱ	3.60.20.10. 3 hits.
HAMAPⁱ	MF_01931. PurF. 1 hit.
InterProⁱ	View protein in InterPro IPR017932. GATase_2_dom. IPR029055. Ntn_hydrolases_N. IPR000836. PRibTrfase_dom. IPR029057. PRTase-like. IPR005854. PurF. IPR035584. PurF_N.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13537. GATase_7. 1 hit. PF00156. Pribosyltran. 1 hit.
PIRSFⁱ	PIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMⁱ	SSF53271. SSF53271. 1 hit. SSF56235. SSF56235. 1 hit.
TIGRFAMsⁱ	TIGR01134. purF. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51278. GATASE_TYPE_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

E3ECX2-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSDEITARTL WTGDYYNEGS GKEGLFDKLK EECGVFGVYR HSDAASLAYY 
        60         70         80         90        100
GLHALQHRGE ESAGICVSSG DEFHYHRGMG LVKEVFNKDL MASLTGDIAI 
       110        120        130        140        150
GHVRYSTSGD SKLTNAQPLV FKYRDGDLAV ATNGNIVNAL QIRHELEQGG 
       160        170        180        190        200
SIFQTTSDTE VVAHLIARSS KDLVEAAKDA LKRIVGGFAF LIMTNDKLLV 
       210        220        230        240        250
ASDPNGLRPL TMGRLGDAYL FASESCALET IGAELLRDIE PGELLILDKN 
       260        270        280        290        300
GLHEDRYTED KQRKALCAME YIYFARPDSD LNGANLHAAR KRMGSQLALE 
       310        320        330        340        350
AFVDADLVTG VPDSSISAAI GYAEQTGIPY ELGMIKNKYT GRTFIQPSQE 
       360        370        380        390        400
LREQGVKMKL SAVRRVVEGK RVIMIDDSIV RGTTSRRIVN MLRDAGALEV 
       410        420        430        440        450
HVRITSPPFK NPCFYGIDTP DRRELIASSK TVEEIRQEIN ADSLFFMSAE 
       460        470        480        490 
GLIAAVGGHN EQDYKGGLCL ACFDNDYPTQ VDFKGEEKFG CSC

Length:493

Mass (Da):54,175

Last modified:January 11, 2011 - v1

Checksum:ⁱB0E2327A471F1ACA

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP002213 Genomic DNA. Translation: ADO54841.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_013369475.1. NC_014622.2.

Genome annotation databases

EnsemblBacteriaⁱ	ADO54841; ADO54841; PPSC2_04245.
GeneIDⁱ	25385515.
KEGGⁱ	ppm:PPSC2_04245.
PATRICⁱ	fig\|886882.15.peg.845.

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
E3ECX2	A0A2K1EFA5 A0A0K2F4N9 A0A1C3CPL6 H6CEI6 A0A074L7F7 A0A1A0G507 A0A0F6EVX8 G7W097 A0A1D7MKI6 A0A0D7X0A7 +12	Paenibacillus sp. F4 Paenibacillus peoriae Paenibacillus polymyxa (Bacillus polymyxa) Paenibacillus sp. Aloe-11 Paenibacillus terrae (strain HPL-003) Paenibacillus terrae Paenibacillus jamilae Paenibacillus kribbensis Paenibacillus sp. IHB B 3084 Paenibacillus polymyxa (strain E681) And more	493	UniRef90_E3ECX2	Cluster: Amidophosphoribosyltransferase	23

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
E3ECX2	P35853 A0A0K1L0E3 A0A2I5MJD0 A0A0E2LU78 A0A0C9QFQ1 S2SAJ2 K6S7Q1 UPI00034347E2 S2QYU8 S2R893 +465	Lactobacillus casei Lactobacillus paracasei Lactobacillus paracasei subsp. paracasei Lactobacillus casei 5b Lactobacillus paracasei NRIC 1981 Lactobacillus paracasei subsp. paracasei Lpp126 Lactobacillus casei UW4 Lactobacillus paracasei subsp. paracasei Lpp14 Lactobacillus paracasei subsp. paracasei Lpp41 Lactobacillus paracasei subsp. paracasei Lpp123 And more	194	UniRef50_P35853	Cluster: Amidophosphoribosyltransferase (Fragment)	476

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP002213 Genomic DNA. Translation: ADO54841.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_013369475.1. NC_014622.2.

3D structure databases

ProteinModelPortalⁱ	E3ECX2.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	886882.PPSC2_c0858.

STRINGⁱ

886882.PPSC2_c0858.

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	C44.001.

MEROPSⁱ

C44.001.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	ADO54841; ADO54841; PPSC2_04245.
GeneIDⁱ	25385515.
KEGGⁱ	ppm:PPSC2_04245.
PATRICⁱ	fig\|886882.15.peg.845.

Phylogenomic databases

eggNOGⁱ	ENOG4105CBA. Bacteria. COG0034. LUCA.
HOGENOMⁱ	HOG000033688.
KEGG Orthology (KO) More...KOⁱ	K00764.
OMAⁱ	FRPLCLG.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H0061.

Enzyme and pathway databases

UniPathwayⁱ	UPA00074; UER00124.
BioCycⁱ	PPOL886882:G1GOE-865-MONOMER.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00715. GPATase_N. 1 hit. cd06223. PRTases_typeI. 1 hit.
Gene3Dⁱ	3.60.20.10. 3 hits.
HAMAPⁱ	MF_01931. PurF. 1 hit.
InterProⁱ	View protein in InterPro IPR017932. GATase_2_dom. IPR029055. Ntn_hydrolases_N. IPR000836. PRibTrfase_dom. IPR029057. PRTase-like. IPR005854. PurF. IPR035584. PurF_N.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13537. GATase_7. 1 hit. PF00156. Pribosyltran. 1 hit.
PIRSFⁱ	PIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMⁱ	SSF53271. SSF53271. 1 hit. SSF56235. SSF56235. 1 hit.
TIGRFAMsⁱ	TIGR01134. purF. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51278. GATASE_TYPE_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	E3ECX2_PAEPS
Accessionⁱ	E3ECX2Primary (citable) accession number: E3ECX2
Entry historyⁱ	Integrated into UniProtKB/TrEMBL:	January 11, 2011
	Last sequence update:	January 11, 2011
	Last modified:	March 28, 2018
	This is version 61 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Unreviewed (UniProtKB/TrEMBL)

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteomeImported

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - E3ECX2 (E3ECX2_PAEPS)

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Amidophosphoribosyltransferase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: IMP biosynthesis via de novo pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

Pathwayⁱ: IMP biosynthesis via de novo pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ