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P10182 (ASPQ_PSES7) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 72. 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:
Glutaminase-asparaginase
EC=3.5.1.38
Alternative name(s):
L-ASNase/L-GLNase
L-asparagine/L-glutamine amidohydrolase
Short name=PGA
Gene names
Name:ansB
OrganismPseudomonas sp. (strain 7A)
Taxonomic identifier313 [NCBI]
Taxonomic lineageBacteria › Proteobacteria

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3.

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

Subunit structure

Homotetramer. Ref.4

Subcellular location

Periplasm.

Sequence similarities

Belongs to the asparaginase 1 family.

Ontologies

Keywords
   Cellular componentPeriplasm
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processasparagine metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionasparaginase activity

Inferred from electronic annotation. Source: InterPro

glutamin-(asparagin-)ase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Glutaminase-asparaginase
PRO_0000171089

Regions

Region100 – 1012Substrate binding By similarity

Sites

Active site201Acyl-ester intermediate Ref.4
Binding site671Substrate By similarity

Experimental info

Sequence conflict71Q → H AA sequence Ref.2
Sequence conflict121V → R AA sequence Ref.2

Secondary structure

1 ............................................................... 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10182 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 11DEEC467CB1475E

FASTA33736,200
        10         20         30         40         50         60 
KEVENQQKLA NVVILATGGT IAGAGASAAN SATYQAAKVG VDKLIAGVPE LADLANVRGE 

        70         80         90        100        110        120 
QVMQIASESI TNDDLLKLGK RVAELADSND VDGIVITHGT DTLEETAYFL DLTLNTDKPI 

       130        140        150        160        170        180 
VVVGSMRPGT AMSADGMLNL YNAVAVASNK DSRGKGVLVT MNDEIQSGRD VSKSINIKTE 

       190        200        210        220        230        240 
AFKSAWGPLG MVVEGKSYWF RLPAKRHTVN SEFDIKQISS LPQVDIAYSY GNVTDTAYKA 

       250        260        270        280        290        300 
LAQNGAKALI HAGTGNGSVS SRLTPALQTL RKTGTQIIRS SHVNQGGFVL RNAEQPDDKN 

       310        320        330 
DWVVAHDLNP EKARILVELA MVKTQDSKEL QRIFWEY

« Hide

References

[1]"Structural characterization of Pseudomonas 7A glutaminase-asparaginase."
Lubkowski J., Wlodawer A., Ammon H.L., Copeland T.D., Swain A.L.
Biochemistry 33:10257-10265(1994) [PubMed: 8068664] [Abstract]
Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[2]"Amino acid sequence of the diazooxonorleucine binding site of Acinetobacter and Pseudomonas 7A glutaminase-asparaginase enzymes."
Holcenberg J.S., Ericsson L., Roberts J.
Biochemistry 17:411-417(1978) [PubMed: 619999] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-26.
[3]"Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7-A resolution."
Jakob C.G., Lewinski K., Lacount M.W., Roberts J., Lebioda L.
Biochemistry 36:923-931(1997) [PubMed: 9020792] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[4]"Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu."
Ortlund E., Lacount M.W., Lewinski K., Lebioda L.
Biochemistry 39:1199-1204(2000) [PubMed: 10684596] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-337 IN COMPLEXES WITH 6-DIAZO-5-OXO-L-NORLEUCINE AND 5-DIAZO-4-OXO-L-NORVALINE, ACTIVE SITE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJOX-ray2.00A/B8-337[»]
1DJPX-ray1.90A/B8-337[»]
3PGAX-ray2.001/2/3/48-337[»]
4PGAX-ray1.70A/B1-337[»]
ProteinModelPortalP10182.
SMRP10182. Positions 8-337.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004550. AsnASE_II.
IPR006034. Asparaginase/glutaminase.
IPR020827. Asparaginase/glutaminase_CS.
[Graphical view]
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 nameASPQ_PSES7
AccessionPrimary (citable) accession number: P10182
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1995
Last modified: July 27, 2011
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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