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P37528 (PDXT_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamine amidotransferase subunit pdxT
EC=2.6.-.-
Alternative name(s):
Glutamine amidotransferase glutaminase subunit pdxT
Gene names
Name:pdxT
Synonyms:yaaE
Ordered Locus Names:BSU00120
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the hydrolysis of glutamine to glutamate and ammonia. Channels an ammonia molecule to pdxS. HAMAP MF_01615

Pathway

Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. HAMAP MF_01615

Subunit structure

Forms a complex with pdxS.

Miscellaneous

The pathway is different from the classical pdxA-pdxJ pathway. HAMAP MF_01615

Sequence similarities

Belongs to the glutamine amidotransferase pdxT/SNO family.

Ontologies

Keywords
   DomainGlutamine amidotransferase
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196Glutamine amidotransferase subunit pdxT HAMAP MF_01615
PRO_0000135632

Sites

Active site791Nucleophile
Active site1701
Active site1721
Binding site1061Glutamine Potential

Secondary structure

1 ........................................ 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37528 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 91111DEF75257882

FASTA19621,447
        10         20         30         40         50         60 
MLTIGVLGLQ GAVREHIHAI EACGAAGLVV KRPEQLNEVD GLILPGGEST TMRRLIDTYQ 

        70         80         90        100        110        120 
FMEPLREFAA QGKPMFGTCA GLIILAKEIA GSDNPHLGLL NVVVERNSFG RQVDSFEADL 

       130        140        150        160        170        180 
TIKGLDEPFT GVFIRAPHIL EAGENVEVLS EHNGRIVAAK QGQFLGCSFH PELTEDHRVT 

       190 
QLFVEMVEEY KQKALV

« Hide

References

« Hide 'large scale' references
[1]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis."
Belitsky B.R.
J. Bacteriol. 186:1191-1196(2004) [PubMed: 14762015] [Abstract]
Cited for: CHARACTERIZATION.
Strain: 168 / SMY.
[4]"Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis."
Bauer J.A., Bennett E.M., Begley T.P., Ealick S.E.
J. Biol. Chem. 279:2704-2711(2004) [PubMed: 14585832] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D26185 Genomic DNA. Translation: BAA05248.1.
AL009126 Genomic DNA. Translation: CAB11788.1.
PIRS66042.
RefSeqNP_387893.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R9GX-ray2.50A/B1-196[»]
2NV0X-ray1.73A/B1-196[»]
2NV2X-ray2.12B/D/F/H/J/L/N/P/R/T/V/X1-196[»]
ProteinModelPortalP37528.
SMRP37528. Positions 1-196.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-7147884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001583; EBBACP00000001583; EBBACG00000001581.
GeneID939971.
GenomeReviewsGene locus BSU00120 in contig AL009126_GR.
KEGGbsu:BSU00120.
NMPDRfig|224308.1.peg.12.
PATRIC18971483. VBIBacSub10457_0013.

Organism-specific databases

GenoListBSU00120. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000582.
HOGENOMHBG292341.
OMACAGLIML.
PhylomeDBP37528.
ProtClustDBPRK13525.

Enzyme and pathway databases

BioCycBSUB:BSU00120-MONOMER.
MetaCyc:MONOMER-15503.

Family and domain databases

HAMAPMF_01615. PdxT.
[Tree]
InterProIPR002161. Glutamine_amidoTferase_suPdxT.
IPR021196. PdxT/SNO_CS.
[Graphical view]
KOK08681.
PfamPF01174. SNO. 1 hit.
[Graphical view]
PIRSFPIRSF005639. Glut_amidoT_SNO. 1 hit.
TIGRFAMsTIGR03800. PLP_synth_Pdx2. 1 hit.
PROSITEPS01236. PDXT_SNO_1. 1 hit.
PS51130. PDXT_SNO_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXT_BACSU
AccessionPrimary (citable) accession number: P37528
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents