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Protein

Pyridoxal 5'-phosphate synthase subunit PdxT

Gene

pdxT

Organism
Bacillus anthracis (strain CDC 684 / NRRL 3495)
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.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)DescriptionActionsGraphical viewLength
Active sitei79NucleophileUniRule annotation1
Binding sitei106L-glutamineUniRule annotation1
Active sitei170Charge relay systemUniRule annotation1
Active sitei172Charge relay systemUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase
LigandPyridoxal 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
Ordered Locus Names:BAMEG_0017
OrganismiBacillus anthracis (strain CDC 684 / NRRL 3495)
Taxonomic identifieri568206 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001858711 – 196Pyridoxal 5'-phosphate synthase subunit PdxTAdd BLAST196

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliC3LIY8.
SMRiC3LIY8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 49L-glutamine bindingUniRule annotation3
Regioni134 – 135L-glutamine bindingUniRule annotation2

Sequence similaritiesi

Belongs to the glutaminase PdxT/SNO family.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000039949.
KOiK08681.
OMAiVFIRAPI.

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.
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.

C3LIY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKIGVLGLQ GAVREHVKSV EASGAEAVVV KRIEQLEEID GLILPGGEST
60 70 80 90 100
TMRRLIDKYD FMEPLRTFAK SGKPMFGTCA GMILLAKTLI GYDEAHIGAM
110 120 130 140 150
DITVERNAFG RQKDSFEAAL SIKGVGEDFV GVFIRAPYVV DVADDVEVLS
160 170 180 190
THGDRMVAVK QGPFLAASFH PELTDDHRVT AYFVEMVKEA KMKKVV
Length:196
Mass (Da):21,432
Last modified:June 16, 2009 - v1
Checksum:iAF1456D39D482FCB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001215 Genomic DNA. Translation: ACP17328.1.
RefSeqiWP_000238798.1. NC_012581.1.

Genome annotation databases

EnsemblBacteriaiACP17328; ACP17328; BAMEG_0017.
KEGGibah:BAMEG_0017.

Similar proteinsi

Entry informationi

Entry nameiPDXT_BACAC
AccessioniPrimary (citable) accession number: C3LIY8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: June 7, 2017
This is version 53 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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