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O34482 (ASPG2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-asparaginase 2
Short name=L-ASNase 2
EC=3.5.1.1
Alternative name(s):
L-asparagine amidohydrolase 2
Gene names
Name:ansZ
Synonyms:yccC
Ordered Locus Names:BSU02690
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the conversion of L-asparagine to L-aspartate and ammonium. Ref.3

Catalytic activity

L-asparagine + H2O = L-aspartate + NH3.

Subunit structure

Homotetramer By similarity.

Induction

Expression is induced during limiting-nitrogen conditions by the nitrogen regulatory factor TnrA. Ref.3

Miscellaneous

B.subtilis contains two L-asparaginase isoenzymes: L-asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-asparaginase II, a high-affinity secreted enzyme.

Sequence similarities

Belongs to the asparaginase 1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processasparagine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionasparaginase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 375356L-asparaginase 2
PRO_0000171077

Regions

Region141 – 1422Substrate binding By similarity

Sites

Active site611O-isoaspartyl threonine intermediate By similarity
Binding site1081Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O34482 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 95FC5A221CE57B58

FASTA37540,103
        10         20         30         40         50         60 
MKKQRMLVLF TALLFVFTGC SHSPETKESP KEKAQTQKVS SASASEKKDL PNIRILATGG 

        70         80         90        100        110        120 
TIAGADQSKT STTEYKAGVV GVESLIEAVP EMKDIANVSG EQIVNVGSTN IDNKILLKLA 

       130        140        150        160        170        180 
KRINHLLASD DVDGIVVTHG TDTLEETAYF LNLTVKSDKP VVIVGSMRPS TAISADGPSN 

       190        200        210        220        230        240 
LYNAVKVAGA PEAKGKGTLV VLNDRIASAR YVTKTNTTTT DTFKSEEMGF VGTIADDIYF 

       250        260        270        280        290        300 
NNEITRKHTK DTDFSVSNLD ELPQVDIIYG YQNDGSYLFD AAVKAGAKGI VFAGSGNGSL 

       310        320        330        340        350        360 
SDAAEKGADS AVKKGVTVVR STRTGNGVVT PNQDYAEKDL LASNSLNPQK ARMLLMLALT 

       370 
KTNDPQKIQA YFNEY

« Hide

References

« Hide 'large scale' references
[1]"A 32 kb nucleotide sequence from the region of the lincomycin-resistance gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and identification of the site of the lin-2 mutation."
Kumano M., Tamakoshi A., Yamane K.
Microbiology 143:2775-2782(1997) [PubMed: 9274031] [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]"Bacillus subtilis 168 contains two differentially regulated genes encoding L-asparaginase."
Fisher S.H., Wray L.V. Jr.
J. Bacteriol. 184:2148-2154(2002) [PubMed: 11914346] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB000617 Genomic DNA. Translation: BAA22230.1.
AL009126 Genomic DNA. Translation: CAB12063.1.
PIRF69754.
RefSeqNP_388151.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34482.
SMRO34482. Positions 48-375.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000000531; EBBACP00000000531; EBBACG00000000529.
GeneID938392.
GenomeReviewsGene locus BSU02690 in contig AL009126_GR.
KEGGbsu:BSU02690.
NMPDRfig|224308.1.peg.270.
PATRIC18972097. VBIBacSub10457_0277.

Organism-specific databases

GenoListBSU02690. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000510.
HOGENOMHBG497495.
OMAVMVAMND.
PhylomeDBO34482.
ProtClustDBCLSK886632.

Enzyme and pathway databases

BioCycBSUB:BSU02690-MONOMER.

Family and domain databases

InterProIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_CS.
[Graphical view]
KOK01424.
PANTHERPTHR11707. Asp/Glutamnse. 1 hit.
PfamPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSPR00139. ASNGLNASE.
SMARTSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMSSF53774. Asp/Glutamnse. 1 hit.
TIGRFAMsTIGR00520. AsnASE_II. 1 hit.
PROSITEPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASPG2_BACSU
AccessionPrimary (citable) accession number: O34482
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 79 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

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