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Protein

Pyridoxal 5'-phosphate synthase subunit PdxT

Gene

pdxT

Organism
Haemophilus influenzae (strain PittEE)
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 sitei82NucleophileUniRule annotation1
Binding sitei109L-glutamineUniRule annotation1
Active sitei172Charge relay systemUniRule annotation1
Active sitei174Charge 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:CGSHiEE_03815
OrganismiHaemophilus influenzae (strain PittEE)
Taxonomic identifieri374930 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000694611 – 192Pyridoxal 5'-phosphate synthase subunit PdxTAdd BLAST192

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

ProteinModelPortaliA5UBN1.
SMRiA5UBN1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni50 – 52L-glutamine bindingUniRule annotation3
Regioni136 – 137L-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.

A5UBN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGILALQG AFAEHARMLE KLGIESVELR NLKNFQQHYS DLSGLILPGG
60 70 80 90 100
ESTAIGKLLR ELYMLEPIKQ AISSGFPVFG TCAGLILLAK EITSQKESHF
110 120 130 140 150
GTMDIVVERN AYGRQLGSFY TEADCKGVGK IPMTFIRGPI ISSVGKKVNI
160 170 180 190
LATVNNKIVA AQEKNMLVTS FHPELTNNLS LHKYFIDICK VA
Length:192
Mass (Da):21,070
Last modified:July 10, 2007 - v1
Checksum:i52297D26C0EE5579
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000671 Genomic DNA. Translation: ABQ98182.1.

Genome annotation databases

EnsemblBacteriaiABQ98182; ABQ98182; CGSHiEE_03815.
KEGGihip:CGSHiEE_03815.

Similar proteinsi

Entry informationi

Entry nameiPDXT_HAEIE
AccessioniPrimary (citable) accession number: A5UBN1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: July 5, 2017
This is version 63 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