glmS

Functionⁱ

Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.UniRule annotation

Catalytic activityⁱ

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.UniRule annotation

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	2	Nucleophile; for GATase activityUniRule annotation		1
Active siteⁱ	605	For Fru-6P isomerization activityUniRule annotation		1

GO - Molecular functionⁱ

carbohydrate derivative binding Source: InterPro
glutamine-fructose-6-phosphate transaminase (isomerizing) activity Source: UniProtKB-EC

Complete GO annotation...

GO - Biological processⁱ

carbohydrate derivative biosynthetic process Source: InterPro
glutamine metabolic process Source: UniProtKB-KW

Complete GO annotation...

Keywordsⁱ

Molecular function	Aminotransferase, Transferase

Molecular function

Aminotransferase, Transferase

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamine--fructose-6-phosphate aminotransferase [isomerizing]UniRule annotation (EC:2.6.1.16UniRule annotation) Alternative name(s): D-fructose-6-phosphate amidotransferaseUniRule annotation GFATUniRule annotation Glucosamine-6-phosphate synthaseUniRule annotation Hexosephosphate aminotransferaseUniRule annotation L-glutamine--D-fructose-6-phosphate amidotransferaseUniRule annotation
Gene namesⁱ	Name:glmSUniRule annotation Ordered Locus Names:BP0666
Organismⁱ	Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifierⁱ	257313 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella pertussis
Proteomesⁱ	UP000002676 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00164

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedUniRule annotation
ChainⁱPRO_0000135306	2 – 610	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]Add BLAST		609

Interactionⁱ

Subunit structureⁱ

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGⁱ	257313.BP0666.

STRINGⁱ

257313.BP0666.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q7VRZ3.
SMRⁱ	Q7VRZ3.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	2 – 221	Glutamine amidotransferase type-2UniRule annotationAdd BLAST	220
Domainⁱ	286 – 426	SIS 1UniRule annotationAdd BLAST	141
Domainⁱ	459 – 600	SIS 2UniRule annotationAdd BLAST	142

Keywords - Domainⁱ

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGⁱ	ENOG4105C46. Bacteria. COG0449. LUCA.
HOGENOMⁱ	HOG000258898.
KEGG Orthology (KO) More...KOⁱ	K00820.
OMAⁱ	RLDSSTC.

Family and domain databases

Gene3Dⁱ	3.60.20.10. 1 hit.
HAMAPⁱ	MF_00164. GlmS. 1 hit.
InterProⁱ	View protein in InterPro IPR017932. GATase_2_dom. IPR005855. GlmS_trans. IPR029055. Ntn_hydrolases_N. IPR001347. SIS.
PANTHERⁱ	PTHR10937:SF15. PTHR10937:SF15. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01380. SIS. 2 hits.
SUPFAMⁱ	SSF56235. SSF56235. 1 hit.
TIGRFAMsⁱ	TIGR01135. glmS. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51278. GATASE_TYPE_2. 1 hit. PS51464. SIS. 2 hits.

Sequenceⁱ

Sequence statusⁱ: Complete.

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

Q7VRZ3-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MCGIVGAVAQ RDITPILIEG LKRLEYRGYD SCGVALYMDG HLRRTRSTKR 
        60         70         80         90        100
VAELSEQVAE DKLGGFTGIA HTRWATHGIP ATYNAHPHFS AQGKDEPRIA 
       110        120        130        140        150
LVHNGIIENH EELRQELQGV GYVFESQTDT EVIAHLVNHL YAGDLFEAVQ 
       160        170        180        190        200
QAVRRLQGAY AIAVFCRDEP HRVVGARQGS PLVVGLGQNE NFLASDALAL 
       210        220        230        240        250
AGTTDQIIYL EDGDVVDLQL ARVWIVDQAG KQVERKAHTV QVHTGAAELG 
       260        270        280        290        300
PYRHFMQKEI FEQPRAVGDT LQDIESITPE LFGDGAYKVF KEIDSLLILA 
       310        320        330        340        350
CGTSYYAGLT AKYWIESIAR IPVAVEIASE YRYRDSVPNP NALVVTISQS 
       360        370        380        390        400
GETADTLAAL KHVRSLGMQH TLTVCNVVTS AMVRECELAY ITRAGVEIGV 
       410        420        430        440        450
ASTKAFTTQL TALFLLTLAL AQTRGRLTEE QEAEHLKALR HLPAAIGAVL 
       460        470        480        490        500
ALEPQIMAWA DRFASKENAL FLGRGMHYPI ALEGALKLKE ISYIHAEAYP 
       510        520        530        540        550
AGELKHGPLA LVTEHMPVVT IAPKDALLEK LKSNMQEVRA RGGELYVFAD 
       560        570        580        590        600
ADSKIANAEG MHVIRMPEYY GALSPIVHTI PLQLLSYHTA CVRGTDVDKP 
       610
RNLAKSVTVE

Length:610

Mass (Da):66,907

Last modified:January 23, 2007 - v3

Checksum:ⁱA26D402A98EBEC23

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BX640412 Genomic DNA. Translation: CAE44992.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_879503.1. NC_002929.2. WP_010929946.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaⁱ	CAE44992; CAE44992; BP0666.
GeneIDⁱ	2667728.
KEGGⁱ	bpe:BP0666.
PATRICⁱ	fig\|257313.5.peg.713.

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	BX640412 Genomic DNA. Translation: CAE44992.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_879503.1. NC_002929.2. WP_010929946.1. NC_002929.2.

3D structure databases

ProteinModelPortalⁱ	Q7VRZ3.
SMRⁱ	Q7VRZ3.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	257313.BP0666.

STRINGⁱ

257313.BP0666.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	CAE44992; CAE44992; BP0666.
GeneIDⁱ	2667728.
KEGGⁱ	bpe:BP0666.
PATRICⁱ	fig\|257313.5.peg.713.

Phylogenomic databases

eggNOGⁱ	ENOG4105C46. Bacteria. COG0449. LUCA.
HOGENOMⁱ	HOG000258898.
KEGG Orthology (KO) More...KOⁱ	K00820.
OMAⁱ	RLDSSTC.

Family and domain databases

Gene3Dⁱ	3.60.20.10. 1 hit.
HAMAPⁱ	MF_00164. GlmS. 1 hit.
InterProⁱ	View protein in InterPro IPR017932. GATase_2_dom. IPR005855. GlmS_trans. IPR029055. Ntn_hydrolases_N. IPR001347. SIS.
PANTHERⁱ	PTHR10937:SF15. PTHR10937:SF15. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01380. SIS. 2 hits.
SUPFAMⁱ	SSF56235. SSF56235. 1 hit.
TIGRFAMsⁱ	TIGR01135. glmS. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51278. GATASE_TYPE_2. 1 hit. PS51464. SIS. 2 hits.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GLMS_BORPE
Accessionⁱ	Q7VRZ3Primary (citable) accession number: Q7VRZ3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
	Last sequence update:	January 23, 2007
	Last modified:	June 7, 2017
	This is version 87 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q7VRZ3 (GLMS_BORPE)

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Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

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

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

<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 location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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 - Cellular componenti

<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

<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

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

Protocols and materials databases

Genome annotation databases

Phylogenomic 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

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ