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

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	29	NucleophileUniRule annotation	1
Metal bindingⁱ	270	Iron-sulfur (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	317	MagnesiumUniRule annotation	1
Metal bindingⁱ	379	MagnesiumUniRule annotation	1
Metal bindingⁱ	380	MagnesiumUniRule annotation	1
Metal bindingⁱ	416	Iron-sulfur (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	467	Iron-sulfur (4Fe-4S)UniRule annotation	1
Metal bindingⁱ	470	Iron-sulfur (4Fe-4S)UniRule annotation	1

GO - Molecular functionⁱ

4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
amidophosphoribosyltransferase activity Source: UniProtKB-EC
metal ion binding Source: UniProtKB-KW

Complete GO annotation...

GO - Biological processⁱ

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

Complete GO annotation...

Keywordsⁱ

Molecular function	Glycosyltransferase, Transferase
Biological process	Purine biosynthesis
Ligand	4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayⁱ	UPA00074; UER00124.

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 annotation Ordered Locus Names:sll0757
Organismⁱ	Synechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifierⁱ	1111708 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Cyanobacteria › Synechococcales › Merismopediaceae › Synechocystis › Synechocystis sp. PCC 6803
Proteomesⁱ	UP000001425 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
PropeptideⁱPRO_0000029273	1 – 28	By similarityAdd BLAST		28
ChainⁱPRO_0000029274	29 – 495	AmidophosphoribosyltransferaseAdd BLAST		467

Proteomic databases

PRIDEⁱ	Q55621.

PRIDEⁱ

Q55621.

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	1148.SYNGTS_2168.

STRINGⁱ

1148.SYNGTS_2168.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q55621.
SMRⁱ	Q55621.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	29 – 254	Glutamine amidotransferase type-2UniRule annotationAdd BLAST		226

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Glutamine amidotransferase

Phylogenomic databases

HOGENOMⁱ	HOG000033688.
InParanoidⁱ	Q55621.
KEGG Orthology (KO) More...KOⁱ	K00764.
OMAⁱ	HVYFARP.
PhylomeDBⁱ	Q55621.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06223. PRTases_typeI. 1 hit.
Gene3Dⁱ	3.60.20.10. 1 hit.
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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam 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. PS00103. PUR_PYR_PR_TRANSFER. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q55621-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MFPPSSDLTE LNDGQPLSGH HADKPEEACG VFGIYAPEEA VAKLTYFGLY 
        60         70         80         90        100
ALQHRGQESA GIATFAGTTV HCHKDMGLVS QVFQESKLNE MVGTLAVGHT 
       110        120        130        140        150
RYSTTGSSHR VNAQPAVLPT RLGPLALAHN GNLVNTNQLR EALAERGCED 
       160        170        180        190        200
FVTTTDSEMI AVAIANEVDK GKDWVEGTIA ALTLCAGAYS LVIGTPEGII 
       210        220        230        240        250
GVRDPHGIRP LVIGVLEEET PRYVLASETC ALDIIGATYV RTVEAGELVH 
       260        270        280        290        300
ITESGLVSHR LAESADRKLC VFEMIYFSRP DSVVNDESLY TYRMRIGKHL 
       310        320        330        340        350
AKESPVDADL VMGVPDSGIP AAIGFSQASG IPYAEGLIKN RYVGRTFIQP 
       360        370        380        390        400
TQHMREHGIR MKLNPLKDVL AGKRIIIVDD SIVRGTTSRK IVRALREAGA 
       410        420        430        440        450
TEVHMRISSP PVTHPCFYGI DTDSQDQLIA ARLTVAEIAE QIEVDSLAYL 
       460        470        480        490 
SQEGMLLCTG EDISHFCSAC FNGRYPITVP DAVRRSKLML ENITA

Length:495

Mass (Da):53,670

Last modified:November 1, 1996 - v1

Checksum:ⁱ417DC5FB4B21207D

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BA000022 Genomic DNA. Translation: BAA10132.1.
PIRⁱ	S76280.

Genome annotation databases

EnsemblBacteriaⁱ	BAA10132; BAA10132; BAA10132.
KEGGⁱ	syn:sll0757.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BA000022 Genomic DNA. Translation: BAA10132.1.
PIRⁱ	S76280.

3D structure databases

ProteinModelPortalⁱ	Q55621.
SMRⁱ	Q55621.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	1148.SYNGTS_2168.

STRINGⁱ

1148.SYNGTS_2168.

Protein family/group databases

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

MEROPSⁱ

C44.001.

Proteomic databases

PRIDEⁱ	Q55621.

PRIDEⁱ

Q55621.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	BAA10132; BAA10132; BAA10132.
KEGGⁱ	syn:sll0757.

Phylogenomic databases

HOGENOMⁱ	HOG000033688.
InParanoidⁱ	Q55621.
KEGG Orthology (KO) More...KOⁱ	K00764.
OMAⁱ	HVYFARP.
PhylomeDBⁱ	Q55621.

Enzyme and pathway databases

UniPathwayⁱ	UPA00074; UER00124.

UniPathwayⁱ

UPA00074; UER00124.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06223. PRTases_typeI. 1 hit.
Gene3Dⁱ	3.60.20.10. 1 hit.
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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam 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. PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PUR1_SYNY3
Accessionⁱ	Q55621Primary (citable) accession number: Q55621
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
	Last sequence update:	November 1, 1996
	Last modified:	July 5, 2017
	This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q55621 (PUR1_SYNY3)

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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 describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

Proteomic 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

Documents

Functionⁱ

Pathwayⁱ: IMP biosynthesis via de novo pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ