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Protein

Pyridoxal 5'-phosphate synthase subunit PdxT

Gene

pdxT

Organism
Tropheryma whipplei (strain TW08/27) (Whipple's bacillus)
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 sitei106L-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.

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:TW505
OrganismiTropheryma whipplei (strain TW08/27) (Whipple's bacillus)
Taxonomic identifieri218496 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesTropheryma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001356731 – 188Pyridoxal 5'-phosphate synthase subunit PdxTAdd BLAST188

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ83HM6.
SMRiQ83HM6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 48L-glutamine binding3
Regioni132 – 133L-glutamine binding2

Sequence similaritiesi

Belongs to the glutaminase PdxT/SNO family.

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

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.

Q83HM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVGVLSLQG SFYEHLSILS RLNTDHIQVK TSEDLSRVTR LIIPGGESTA
60 70 80 90 100
MLALTQKSGL FDLVRDRIMS GMPVYGTCAG MIMLSTFVED FPNQKTLSCL
110 120 130 140 150
DIAVRRNAFG RQINSFESEV SFLNSKITVP FIRAPKITQI GEGVDVLSRL
160 170 180
ESGDIVAVRQ GNVMATAFHP ELTGGAAVHE YFLHLGLE
Length:188
Mass (Da):20,577
Last modified:June 1, 2003 - v1
Checksum:iB9C24BF371C4E795
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX251411 Genomic DNA. Translation: CAD67172.1.
RefSeqiWP_011096452.1. NC_004551.1.

Genome annotation databases

EnsemblBacteriaiCAD67172; CAD67172; TW505.
KEGGitws:TW505.

Similar proteinsi

Entry informationi

Entry nameiPDXT_TROW8
AccessioniPrimary (citable) accession number: Q83HM6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: November 22, 2017
This is version 77 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