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Protein

L-asparaginase 2

Gene

ansZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of L-asparagine to L-aspartate and ammonium.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei61 – 611O-isoaspartyl threonine intermediatePROSITE-ProRule annotation
Binding sitei108 – 1081SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciBSUB:BSU02690-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
L-asparaginase 2 (EC:3.5.1.1)
Short name:
L-ASNase 2
Alternative name(s):
L-asparagine amidohydrolase 2
Gene namesi
Name:ansZ
Synonyms:yccC
Ordered Locus Names:BSU02690
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 375356L-asparaginase 2PRO_0000171077Add
BLAST

Proteomic databases

PaxDbiO34482.

Expressioni

Inductioni

Expression is induced during limiting-nitrogen conditions by the nitrogen regulatory factor TnrA.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001493.

Structurei

3D structure databases

ProteinModelPortaliO34482.
SMRiO34482. Positions 48-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 375325Asparaginase/glutaminasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni141 – 1422Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the asparaginase 1 family.Curated
Contains 1 asparaginase/glutaminase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107RB3. Bacteria.
COG0252. LUCA.
HOGENOMiHOG000044165.
InParanoidiO34482.
KOiK01424.
OMAiARYITKT.
OrthoDBiEOG6VTK47.
PhylomeDBiO34482.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O34482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKQRMLVLF TALLFVFTGC SHSPETKESP KEKAQTQKVS SASASEKKDL
60 70 80 90 100
PNIRILATGG TIAGADQSKT STTEYKAGVV GVESLIEAVP EMKDIANVSG
110 120 130 140 150
EQIVNVGSTN IDNKILLKLA KRINHLLASD DVDGIVVTHG TDTLEETAYF
160 170 180 190 200
LNLTVKSDKP VVIVGSMRPS TAISADGPSN LYNAVKVAGA PEAKGKGTLV
210 220 230 240 250
VLNDRIASAR YVTKTNTTTT DTFKSEEMGF VGTIADDIYF NNEITRKHTK
260 270 280 290 300
DTDFSVSNLD ELPQVDIIYG YQNDGSYLFD AAVKAGAKGI VFAGSGNGSL
310 320 330 340 350
SDAAEKGADS AVKKGVTVVR STRTGNGVVT PNQDYAEKDL LASNSLNPQK
360 370
ARMLLMLALT KTNDPQKIQA YFNEY
Length:375
Mass (Da):40,103
Last modified:January 1, 1998 - v1
Checksum:i95FC5A221CE57B58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000617 Genomic DNA. Translation: BAA22230.1.
AL009126 Genomic DNA. Translation: CAB12063.1.
PIRiF69754.
RefSeqiNP_388151.1. NC_000964.3.
WP_003246337.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB12063; CAB12063; BSU02690.
GeneIDi938392.
KEGGibsu:BSU02690.
PATRICi18972097. VBIBacSub10457_0277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000617 Genomic DNA. Translation: BAA22230.1.
AL009126 Genomic DNA. Translation: CAB12063.1.
PIRiF69754.
RefSeqiNP_388151.1. NC_000964.3.
WP_003246337.1. NZ_JNCM01000030.1.

3D structure databases

ProteinModelPortaliO34482.
SMRiO34482. Positions 48-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001493.

Proteomic databases

PaxDbiO34482.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12063; CAB12063; BSU02690.
GeneIDi938392.
KEGGibsu:BSU02690.
PATRICi18972097. VBIBacSub10457_0277.

Phylogenomic databases

eggNOGiENOG4107RB3. Bacteria.
COG0252. LUCA.
HOGENOMiHOG000044165.
InParanoidiO34482.
KOiK01424.
OMAiARYITKT.
OrthoDBiEOG6VTK47.
PhylomeDBiO34482.

Enzyme and pathway databases

BioCyciBSUB:BSU02690-MONOMER.

Family and domain databases

Gene3Di3.40.50.1170. 1 hit.
3.40.50.40. 1 hit.
InterProiIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_AS1.
IPR027475. Asparaginase/glutaminase_AS2.
IPR027473. L-asparaginase_C.
IPR027474. L-asparaginase_N.
[Graphical view]
PfamiPF00710. Asparaginase. 1 hit.
[Graphical view]
PIRSFiPIRSF001220. L-ASNase_gatD. 1 hit.
PRINTSiPR00139. ASNGLNASE.
SMARTiSM00870. Asparaginase. 1 hit.
[Graphical view]
SUPFAMiSSF53774. SSF53774. 1 hit.
TIGRFAMsiTIGR00520. asnASE_II. 1 hit.
PROSITEiPS00144. ASN_GLN_ASE_1. 1 hit.
PS00917. ASN_GLN_ASE_2. 1 hit.
PS51732. ASN_GLN_ASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiASPG2_BACSU
AccessioniPrimary (citable) accession number: O34482
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.