Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyridoxal 5'-phosphate synthase subunit PdxT

Gene

pdxT

Organism
Mycobacterium sp. (strain JLS)
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 sitei91Nucleophile1
Binding sitei123L-glutamine1
Active sitei187Charge relay system1
Active sitei189Charge 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:Mjls_2289
OrganismiMycobacterium sp. (strain JLS)
Taxonomic identifieri164757 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002930051 – 206Pyridoxal 5'-phosphate synthase subunit PdxTAdd BLAST206

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliA3PYU8.
SMRiA3PYU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni59 – 61L-glutamine binding3
Regioni151 – 152L-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.

A3PYU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAVPDGRSD KPRSVVGVLA LQGDTREHLA ALTEAGAEAV TVRRLRELEA
60 70 80 90 100
VDALVIPGGE STAMSHLLRE FELLEPLRAR LAEGMPAYGS CAGMILLATE
110 120 130 140 150
ILDAGAAGRE ATPLKGIDMS VRRNAFGRQV DSFEGDIPFV GLDSSVHAVF
160 170 180 190 200
IRAPWVERIG DGVEVLARAD GHIVAVRQGR MLATAFHPEV TGDRRVHKLF

VDMVSE
Length:206
Mass (Da):22,130
Last modified:April 3, 2007 - v1
Checksum:iECFF7C749E109D6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000580 Genomic DNA. Translation: ABN98075.1.
RefSeqiWP_011855492.1. NC_009077.1.

Genome annotation databases

EnsemblBacteriaiABN98075; ABN98075; Mjls_2289.
KEGGimjl:Mjls_2289.

Similar proteinsi

Entry informationi

Entry nameiPDXT_MYCSJ
AccessioniPrimary (citable) accession number: A3PYU8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: April 3, 2007
Last modified: November 22, 2017
This is version 62 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