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Protein

Pyridoxal 5'-phosphate synthase subunit PdxT

Gene

pdxT

Organism
Geobacillus thermodenitrificans (strain NG80-2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.

Catalytic activityi

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

Pathwayi: pyridoxal 5'-phosphate biosynthesis

This protein is involved in the pathway pyridoxal 5'-phosphate biosynthesis, which is part of Cofactor biosynthesis.
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)DescriptionActionsGraphical viewLength
Active sitei78Nucleophile1
Binding sitei105L-glutamine1
Active sitei169Charge relay system1
Active sitei171Charge relay system1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase
LigandPyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00245.

Protein family/group databases

MEROPSiC26.A32.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal 5'-phosphate synthase subunit PdxT (EC:4.3.3.6)
Alternative name(s):
Pdx2
Pyridoxal 5'-phosphate synthase glutaminase subunit (EC:3.5.1.2)
Gene namesi
Name:pdxT
Ordered Locus Names:GTNG_0012
OrganismiGeobacillus thermodenitrificans (strain NG80-2)
Taxonomic identifieri420246 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
Proteomesi
  • UP000001578 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000694601 – 195Pyridoxal 5'-phosphate synthase subunit PdxTAdd BLAST195

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi420246.GTNG_0012.

Structurei

3D structure databases

ProteinModelPortaliA4IJ95.
SMRiA4IJ95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 48L-glutamine binding3
Regioni133 – 134L-glutamine binding2

Sequence similaritiesi

Belongs to the glutaminase PdxT/SNO family.

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4108UHX. Bacteria.
COG0311. LUCA.
HOGENOMiHOG000039949.
KOiK08681.
OMAiVFIRAPI.
OrthoDBiPOG091H084H.

Family and domain databases

CDDicd01749. GATase1_PB. 1 hit.
Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_01615. PdxT. 1 hit.
InterProiView protein in InterPro
IPR029062. Class_I_gatase-like.
IPR002161. PdxT/SNO.
IPR021196. PdxT/SNO_CS.
PANTHERiPTHR31559. PTHR31559. 1 hit.
PfamiView protein in Pfam
PF01174. SNO. 1 hit.
PIRSFiPIRSF005639. Glut_amidoT_SNO. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR03800. PLP_synth_Pdx2. 1 hit.
PROSITEiView protein in PROSITE
PS01236. PDXT_SNO_1. 1 hit.
PS51130. PDXT_SNO_2. 1 hit.

Sequencei

Sequence statusi: Complete.

A4IJ95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGVLGLQG AVQEHVRAIE ACGAEAVVVK KTEQLTGLDG LVLPGGESTT
60 70 80 90 100
MRRLIDRYGL MEPLKQFAAD GKPMFGTCAG LILLAKRIVG YDEPHLGLMD
110 120 130 140 150
ITVERNSFGR QRESFEAELS IKGVGDGFVG VFIRAPHIVE VGDEVEVLAT
160 170 180 190
YNDRIVAARQ GQFLGCSFHP ELTDDHRLMR YFLNMVKEAK TVSSI
Length:195
Mass (Da):21,364
Last modified:May 1, 2007 - v1
Checksum:iA7BB994877D70F22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO65399.1.
RefSeqiWP_008882086.1. NC_009328.1.

Genome annotation databases

EnsemblBacteriaiABO65399; ABO65399; GTNG_0012.
GeneIDi31759218.
KEGGigtn:GTNG_0012.

Similar proteinsi

Entry informationi

Entry nameiPDXT_GEOTN
AccessioniPrimary (citable) accession number: A4IJ95
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 2007
Last modified: November 22, 2017
This is version 67 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families