pdxT

Functionⁱ

Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.

UniRule annotation1 Publication

Catalytic activityⁱ

aldehydo-D-ribose 5-phosphate
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+
D-glyceraldehyde 3-phosphate
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+
L-glutamine
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=
H⁺
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+ 3
H₂O
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+
L-glutamate
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+
phosphate
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+
pyridoxal 5'-phosphate
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UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_01615
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis."
  Raschle T., Amrhein N., Fitzpatrick T.B.
  J. Biol. Chem. 280:32291-32300(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 74-87, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION OF REACTION PRODUCT, IDENTIFICATION OF ACTIVE SITE CYS.
EC:
4.3.3.6
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_01615
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis."
  Raschle T., Amrhein N., Fitzpatrick T.B.
  J. Biol. Chem. 280:32291-32300(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 74-87, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION OF REACTION PRODUCT, IDENTIFICATION OF ACTIVE SITE CYS.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
aldehydo-D-ribose 5-phosphate
zoom
+
D-glyceraldehyde 3-phosphate
zoom
+
L-glutamine
zoom
=
H⁺
+
3
H₂O
+
L-glutamate
zoom
+
phosphate
zoom
+
pyridoxal 5'-phosphate
zoom
H₂O
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
L-glutamine
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See the description of this molecule in ChEBI.
=
L-glutamate
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+
NH₄⁺
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UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_01615
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis."
  Raschle T., Amrhein N., Fitzpatrick T.B.
  J. Biol. Chem. 280:32291-32300(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 74-87, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION OF REACTION PRODUCT, IDENTIFICATION OF ACTIVE SITE CYS.
EC:
3.5.1.2
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_01615
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis."
  Raschle T., Amrhein N., Fitzpatrick T.B.
  J. Biol. Chem. 280:32291-32300(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 74-87, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION OF REACTION PRODUCT, IDENTIFICATION OF ACTIVE SITE CYS.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
+
L-glutamine
zoom
=
L-glutamate
zoom
+
NH₄⁺
zoom

Kineticsⁱ

kcat is 7.60 min(-1) for glutaminase activity.1 Publication

K_M=
0.99 mM for L-glutamine
1 Publication
Manual assertion based on experiment inⁱ
Ref.3
"On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis."
Raschle T., Amrhein N., Fitzpatrick T.B.
J. Biol. Chem. 280:32291-32300(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 74-87, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION OF REACTION PRODUCT, IDENTIFICATION OF ACTIVE SITE CYS.

Pathwayⁱ: pyridoxal 5'-phosphate biosynthesis

This protein is involved in the pathway pyridoxal 5'-phosphate biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway pyridoxal 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	79	NucleophileUniRule annotationCurated	1
Binding siteⁱ	106	L-glutamineUniRule annotation1 Publication	1
Active siteⁱ	170	Charge relay systemUniRule annotationCurated	1
Active siteⁱ	172	Charge relay systemUniRule annotationCurated	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Lyase
Ligand	Pyridoxal phosphate

Enzyme and pathway databases

BioCycⁱ	BSUB:BSU00120-MONOMER
BRENDAⁱ	4.3.3.6, 658
UniPathwayⁱ	UPA00245

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Pyridoxal 5'-phosphate synthase subunit PdxTUniRule annotation (EC:4.3.3.6UniRule annotation1 Publication) Alternative name(s): Pdx2UniRule annotation Pyridoxal 5'-phosphate synthase glutaminase subunitUniRule annotation (EC:3.5.1.2UniRule annotation1 Publication)
Gene namesⁱ	Name:pdxTUniRule annotation Synonyms:yaaE Ordered Locus Names:BSU00120
Organismⁱ	Bacillus subtilis (strain 168)
Taxonomic identifierⁱ	224308 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis
Proteomesⁱ	UP000001570 Componentⁱ: Chromosome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10	Q → A: 3-fold reduction in glutaminase activity. 1 Publication	1
Mutagenesisⁱ	10	Q → E: Almost no activity. 1 Publication	1
Mutagenesisⁱ	10	Q → N: 10-fold reduction in glutaminase activity. 1 Publication	1
Mutagenesisⁱ	15	E → A: Almost no effect on glutaminase activity. 1 Publication	1
Mutagenesisⁱ	48	E → A: No activity, disturbing interaction with PdxS. 1 Publication	1
Mutagenesisⁱ	106	R → A: No activity, disturbing interaction with PdxS. 1 Publication	1
Mutagenesisⁱ	135	R → A: No activity, disturbing interaction with PdxS. 1 Publication	1
Mutagenesisⁱ	170	H → N: No activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000135632	1 – 196	Pyridoxal 5'-phosphate synthase subunit PdxTAdd BLAST		196

Proteomic databases

PaxDbⁱ	P37528

PaxDbⁱ

P37528

Interactionⁱ

Subunit structureⁱ

In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.

UniRule annotation1 Publication

Binary interactionsⁱ

Hide details

P37528

With	#Exp.	IntAct
pdxS [P37527]	5	EBI-7051766,EBI-7828661
itself	2	EBI-7051766,EBI-7051766

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-57719N
IntActⁱ	P37528, 2 interactors
Molecular INTeraction database More...MINTⁱ	P37528
STRINGⁱ	224308.BSU00120

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 7	Combined sources	5
Beta strandⁱ	9 – 11	Combined sources	3
Helixⁱ	14 – 22	Combined sources	9
Beta strandⁱ	26 – 30	Combined sources	5
Helixⁱ	33 – 38	Combined sources	6
Beta strandⁱ	40 – 44	Combined sources	5
Helixⁱ	49 – 58	Combined sources	10
Helixⁱ	62 – 70	Combined sources	9
Beta strandⁱ	75 – 78	Combined sources	4
Helixⁱ	80 – 85	Combined sources	6
Beta strandⁱ	86 – 89	Combined sources	4
Beta strandⁱ	102 – 105	Combined sources	4
Turnⁱ	106 – 109	Combined sources	4
Turnⁱ	111 – 113	Combined sources	3
Beta strandⁱ	114 – 120	Combined sources	7
Beta strandⁱ	129 – 135	Combined sources	7
Beta strandⁱ	138 – 142	Combined sources	5
Beta strandⁱ	147 – 152	Combined sources	6
Beta strandⁱ	155 – 161	Combined sources	7
Beta strandⁱ	164 – 169	Combined sources	6
Beta strandⁱ	173 – 175	Combined sources	3
Helixⁱ	178 – 193	Combined sources	16

Show more details

3D structure databases

SMRⁱ	P37528
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P37528

EvolutionaryTraceⁱ

P37528

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	47 – 49	L-glutamine bindingUniRule annotation1 Publication		3
Regionⁱ	134 – 135	L-glutamine bindingUniRule annotation1 Publication		2

Sequence similaritiesⁱ

Belongs to the glutaminase PdxT/SNO family.UniRule annotation

Keywords - Domainⁱ

Glutamine amidotransferase

Phylogenomic databases

eggNOGⁱ	COG0311, Bacteria
InParanoidⁱ	P37528
OMAⁱ	VFIRAPI
PhylomeDBⁱ	P37528

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01749, GATase1_PB, 1 hit
Gene3Dⁱ	3.40.50.880, 1 hit
HAMAPⁱ	MF_01615, PdxT, 1 hit
InterProⁱ	View protein in InterPro IPR029062, Class_I_gatase-like IPR002161, PdxT/SNO IPR021196, PdxT/SNO_CS
PANTHERⁱ	PTHR31559, PTHR31559, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01174, SNO, 1 hit
PIRSFⁱ	PIRSF005639, Glut_amidoT_SNO, 1 hit
SUPFAMⁱ	SSF52317, SSF52317, 1 hit
TIGRFAMsⁱ	TIGR03800, PLP_synth_Pdx2, 1 hit
PROSITEⁱ	View protein in PROSITE PS01236, PDXT_SNO_1, 1 hit PS51130, PDXT_SNO_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P37528-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLTIGVLGLQ GAVREHIHAI EACGAAGLVV KRPEQLNEVD GLILPGGEST 
        60         70         80         90        100
TMRRLIDTYQ FMEPLREFAA QGKPMFGTCA GLIILAKEIA GSDNPHLGLL 
       110        120        130        140        150
NVVVERNSFG RQVDSFEADL TIKGLDEPFT GVFIRAPHIL EAGENVEVLS 
       160        170        180        190 
EHNGRIVAAK QGQFLGCSFH PELTEDHRVT QLFVEMVEEY KQKALV

Length:196

Mass (Da):21,447

Last modified:October 1, 1994 - v1

Checksum:ⁱ91111DEF75257882

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D26185 Genomic DNA Translation: BAA05248.1 AL009126 Genomic DNA Translation: CAB11788.1
PIRⁱ	S66042
NCBI Reference Sequences More...RefSeqⁱ	NP_387893.1, NC_000964.3 WP_003226797.1, NZ_JNCM01000024.1

Genome annotation databases

EnsemblBacteriaⁱ	CAB11788; CAB11788; BSU_00120
GeneIDⁱ	939971
KEGGⁱ	bsu:BSU00120
PATRICⁱ	fig\|224308.179.peg.12

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P37528	Pyridoxal 5'-phosphate synthase subunit PdxT		BACSU		196	UniRef100_P37528
Pyridoxal 5'-phosphate synthase glutaminase subunit PdxT		Bacillus sp. LJBS17		196
Pyridoxal 5'-phosphate synthase subunit PdxT		BACIU		196
Pyridoxal 5'-phosphate synthase subunit PdxT		BACNB		196
Pyridoxal 5'-phosphate synthase subunit PdxT		Bacillus subtilis subsp. subtilis str. SC-8		196
+4

Protein	Similar proteins		Species	Score	Length	Source
P37528	Pyridoxal 5'-phosphate synthase subunit PdxT		BACSU		196	UniRef90_P37528
Pyridoxal 5'-phosphate synthase glutaminase subunit PdxT		Bacillus sp. LJBS17		196
Pyridoxal 5'-phosphate synthase subunit PdxT		BACIU		196
Pyridoxal 5'-phosphate synthase subunit PdxT		BACNB		196
Pyridoxal 5'-phosphate synthase subunit PdxT		Bacillus subtilis subsp. subtilis str. SC-8		196
+82

Protein	Similar proteins		Species	Score	Length	Source
P37528	Pyridoxal 5'-phosphate synthase subunit PdxT		OENOB		191	UniRef50_P37528
Pyridoxal 5'-phosphate synthase subunit PdxT		EXIS2		192
Pyridoxal 5'-phosphate synthase subunit PdxT		STAEQ		186
Pyridoxal 5'-phosphate synthase subunit PdxT		STAES		185
Pyridoxal 5'-phosphate synthase subunit PdxT		BACCN		196
+2655

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D26185 Genomic DNA Translation: BAA05248.1 AL009126 Genomic DNA Translation: CAB11788.1
PIRⁱ	S66042
RefSeqⁱ	NP_387893.1, NC_000964.3 WP_003226797.1, NZ_JNCM01000024.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1R9G	X-ray	2.50	A/B	1-196	[»]
	2NV0	X-ray	1.73	A/B	1-196	[»]
	2NV2	X-ray	2.12	B/D/F/H/J/L/N/P/R/T/V/X	1-196	[»]
SMRⁱ	P37528
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

DIPⁱ	DIP-57719N
IntActⁱ	P37528, 2 interactors
MINTⁱ	P37528
STRINGⁱ	224308.BSU00120

Proteomic databases

PaxDbⁱ	P37528

PaxDbⁱ

P37528

Genome annotation databases

EnsemblBacteriaⁱ	CAB11788; CAB11788; BSU_00120
GeneIDⁱ	939971
KEGGⁱ	bsu:BSU00120
PATRICⁱ	fig\|224308.179.peg.12

Phylogenomic databases

eggNOGⁱ	COG0311, Bacteria
InParanoidⁱ	P37528
OMAⁱ	VFIRAPI
PhylomeDBⁱ	P37528

Enzyme and pathway databases

UniPathwayⁱ	UPA00245
BioCycⁱ	BSUB:BSU00120-MONOMER
BRENDAⁱ	4.3.3.6, 658

Miscellaneous databases

EvolutionaryTraceⁱ	P37528

EvolutionaryTraceⁱ

P37528

Family and domain databases

CDDⁱ	cd01749, GATase1_PB, 1 hit
Gene3Dⁱ	3.40.50.880, 1 hit
HAMAPⁱ	MF_01615, PdxT, 1 hit
InterProⁱ	View protein in InterPro IPR029062, Class_I_gatase-like IPR002161, PdxT/SNO IPR021196, PdxT/SNO_CS
PANTHERⁱ	PTHR31559, PTHR31559, 1 hit
Pfamⁱ	View protein in Pfam PF01174, SNO, 1 hit
PIRSFⁱ	PIRSF005639, Glut_amidoT_SNO, 1 hit
SUPFAMⁱ	SSF52317, SSF52317, 1 hit
TIGRFAMsⁱ	TIGR03800, PLP_synth_Pdx2, 1 hit
PROSITEⁱ	View protein in PROSITE PS01236, PDXT_SNO_1, 1 hit PS51130, PDXT_SNO_2, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PDXT_BACSU
Accessionⁱ	P37528Primary (citable) accession number: P37528
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
	Last sequence update:	October 1, 1994
	Last modified:	February 23, 2022
	This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Uncharacterized protein families (UPF)
List of uncharacterized protein family (UPF) entries
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P37528 (PDXT_BACSU)

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Pyridoxal 5'-phosphate synthase subunit PdxT

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%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: pyridoxal 5'-phosphate biosynthesis

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

GO - Biological processi

Enzyme and pathway 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 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

Cytosol

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<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

P37528

GO - Molecular functioni

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

Secondary structure

3D structure databases

Miscellaneous 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

Region

<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

Keywords - Domaini

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

Proteomic databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Pathwayⁱ: pyridoxal 5'-phosphate biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ