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Protein

Pyridoxal 5'-phosphate synthase subunit PdxT

Gene

pdxT

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 annotation

Catalytic activityi

D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate.UniRule annotation
L-glutamine + H2O = L-glutamate + NH3.UniRule annotation

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei78 – 781NucleophileUniRule annotation
Binding sitei105 – 1051L-glutamineUniRule annotation
Active sitei169 – 1691Charge relay systemUniRule annotation
Active sitei171 – 1711Charge relay systemUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00245.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal 5'-phosphate synthase subunit PdxTUniRule annotation (EC:4.3.3.6UniRule annotation)
Alternative name(s):
Pdx2UniRule annotation
Pyridoxal 5'-phosphate synthase glutaminase subunitUniRule annotation (EC:3.5.1.2UniRule annotation)
Gene namesi
Name:pdxTUniRule annotation
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Pyridoxal 5'-phosphate synthase subunit PdxTPRO_0000135631Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi9 – 113Combined sources
Helixi13 – 219Combined sources
Beta strandi25 – 295Combined sources
Helixi32 – 354Combined sources
Beta strandi39 – 435Combined sources
Helixi48 – 5710Combined sources
Helixi61 – 699Combined sources
Beta strandi74 – 774Combined sources
Helixi80 – 845Combined sources
Beta strandi85 – 917Combined sources
Beta strandi99 – 1046Combined sources
Helixi106 – 1094Combined sources
Beta strandi115 – 1217Combined sources
Turni122 – 1243Combined sources
Beta strandi125 – 13410Combined sources
Beta strandi137 – 1415Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi154 – 1607Combined sources
Beta strandi163 – 1686Combined sources
Helixi170 – 1723Combined sources
Helixi177 – 19519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7RX-ray1.90A1-196[»]
ProteinModelPortaliP83813.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83813.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 483L-glutamine bindingUniRule annotation
Regioni133 – 1342L-glutamine bindingUniRule annotation

Sequence similaritiesi

Belongs to the glutaminase PdxT/SNO family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_01615. PdxT.
InterProiIPR029062. Class_I_gatase-like.
IPR002161. PdxT/SNO.
IPR021196. PdxT/SNO_CS.
[Graphical view]
PfamiPF01174. SNO. 1 hit.
[Graphical view]
PIRSFiPIRSF005639. Glut_amidoT_SNO. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR03800. PLP_synth_Pdx2. 1 hit.
PROSITEiPS01236. PDXT_SNO_1. 1 hit.
PS51130. PDXT_SNO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGVLGLQG AVREHVRAIE ACGAEAVIVK KSEQLEGLDG LVLPGGESTT
60 70 80 90 100
XRRLIDRYGL XEPLKQFAAA GKPXFGTCAG LILLAKRIVG YDEPHLGLXD
110 120 130 140 150
ITVERNSFGR QRESFEAELS IKGVGDGFVG VFIRAPHIVE AGDGVDVLAT
160 170 180 190
YNDRIVAARQ GQFLGCSFHP ELTDDHRLXQ YFLNXVKEAK XASSLK
Length:196
Mass (Da):21,225
Last modified:March 15, 2004 - v1
Checksum:iFAE3D389E229A41B
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7RX-ray1.90A1-196[»]
ProteinModelPortaliP83813.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00245.

Miscellaneous databases

EvolutionaryTraceiP83813.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_01615. PdxT.
InterProiIPR029062. Class_I_gatase-like.
IPR002161. PdxT/SNO.
IPR021196. PdxT/SNO_CS.
[Graphical view]
PfamiPF01174. SNO. 1 hit.
[Graphical view]
PIRSFiPIRSF005639. Glut_amidoT_SNO. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR03800. PLP_synth_Pdx2. 1 hit.
PROSITEiPS01236. PDXT_SNO_1. 1 hit.
PS51130. PDXT_SNO_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "X-ray structure analysis of a predicted amidotransferase from B.stearothermophilus at 1.9 A resolution."
    Miller D.J., Anderson W.F.
    Submitted (AUG-2003) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiPDXT_GEOSE
AccessioniPrimary (citable) accession number: P83813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: March 15, 2004
Last modified: June 24, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The sequence shown here has been extracted from PDB entry 1Q7R.Curated

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.