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P37527 (PDXS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyridoxal biosynthesis lyase pdxS
EC=4.-.-.-
Alternative name(s):
Superoxide-inducible protein 7
Short name=SOI7
Gene names
Name:pdxS
Synonyms:yaaD
Ordered Locus Names:BSU00110
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the production of pyridoxal phosphate, probably by incorporating ammonia into the pyridine ring. HAMAP MF_01824

Pathway

Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. HAMAP MF_01824

Subunit structure

Forms a complex with pdxT.

Induction

By superoxide. HAMAP MF_01824

Post-translational modification

Can be guanylylated in vitro. HAMAP MF_01824

Miscellaneous

The pathway is different from the classical pdxA-pdxJ pathway. HAMAP MF_01824

Sequence similarities

Belongs to the pdxS/SNZ family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processpyridoxal phosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionlyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 294293Pyridoxal biosynthesis lyase pdxS HAMAP MF_01824
PRO_0000109383

Experimental info

Sequence conflict301Q → D AA sequence Ref.4

Secondary structure

1 .............................................. 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37527 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1662DA1925DDA9B1

FASTA29431,612
        10         20         30         40         50         60 
MAQTGTERVK RGMAEMQKGG VIMDVINAEQ AKIAEEAGAV AVMALERVPA DIRAAGGVAR 

        70         80         90        100        110        120 
MADPTIVEEV MNAVSIPVMA KARIGHIVEA RVLEAMGVDY IDESEVLTPA DEEFHLNKNE 

       130        140        150        160        170        180 
YTVPFVCGCR DLGEATRRIA EGASMLRTKG EPGTGNIVEA VRHMRKVNAQ VRKVVAMSED 

       190        200        210        220        230        240 
ELMTEAKNLG APYELLLQIK KDGKLPVVNF AAGGVATPAD AALMMQLGAD GVFVGSGIFK 

       250        260        270        280        290 
SDNPAKFAKA IVEATTHFTD YKLIAELSKE LGTAMKGIEI SNLLPEQRMQ ERGW

« 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]"Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation."
Mitchell C., Morris P.W., Vary J.C.
Mol. Microbiol. 6:1579-1581(1992) [PubMed: 1495386] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
Strain: 168 / DB100.
[4]"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis."
Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.
Electrophoresis 18:1451-1463(1997) [PubMed: 9298659] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-32.
Strain: 168 / IS58.
[5]"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.
[6]"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: MODEL OF PDXS-PDXT COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB11787.1.
PIRS66041.
RefSeqNP_387892.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NV1X-ray2.08A/B/C/D/E/F1-294[»]
2NV2X-ray2.12A/C/E/G/I/K/M/O/Q/S/U/W1-294[»]
ProteinModelPortalP37527.
SMRP37527. Positions 2-272.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002785; EBBACP00000002785; EBBACG00000002780.
GeneID939988.
GenomeReviewsGene locus BSU00110 in contig AL009126_GR.
KEGGbsu:BSU00110.
PATRIC18971481. VBIBacSub10457_0012.

Organism-specific databases

GenoListBSU00110. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000844.
HOGENOMHBG292342.
OMARIWEGAA.
PhylomeDBP37527.
ProtClustDBPRK04180.

Enzyme and pathway databases

BioCycBSUB:BSU00110-MONOMER.
MetaCyc:MONOMER-15502.

Family and domain databases

HAMAPMF_01824. PdxS.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR001852. Snz1p/Sor1.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 2 hits.
KOK06215.
PANTHERPTHR22854:SF9. PTHR22854:SF9. 1 hit.
PfamPF01680. SOR_SNZ. 1 hit.
[Graphical view]
PIRSFPIRSF029271. Pdx1. 1 hit.
SUPFAMSSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR00343. TIGR00343. 1 hit.
PROSITEPS01235. PDXS_SNZ_1. 1 hit.
PS51129. PDXS_SNZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDXS_BACSU
AccessionPrimary (citable) accession number: P37527
Secondary accession number(s): P27877
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

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