Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutaminase-asparaginase

Gene

ansB

Organism
Pseudomonas sp. (strain ATCC 29598 / 7A)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei20 – 201Acyl-ester intermediatePROSITE-ProRule annotation1 Publication
Binding sitei67 – 671SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.5.1.38. 5085.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaminase-asparaginase (EC:3.5.1.38)
Alternative name(s):
L-ASNase/L-GLNase
L-asparagine/L-glutamine amidohydrolase
Short name:
PGA
Gene namesi
Name:ansB
OrganismiPseudomonas sp. (strain ATCC 29598 / 7A)
Taxonomic identifieri313 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Glutaminase-asparaginasePRO_0000171089Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
337
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 199Combined sources
Helixi20 – 223Combined sources
Beta strandi26 – 294Combined sources
Beta strandi31 – 377Combined sources
Helixi41 – 466Combined sources
Helixi51 – 544Combined sources
Beta strandi56 – 6510Combined sources
Helixi67 – 693Combined sources
Helixi72 – 8716Combined sources
Beta strandi92 – 976Combined sources
Helixi100 – 1023Combined sources
Helixi103 – 11311Combined sources
Beta strandi120 – 1234Combined sources
Helixi136 – 14712Combined sources
Helixi150 – 1523Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi164 – 1674Combined sources
Turni168 – 1703Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi196 – 1994Combined sources
Beta strandi201 – 2033Combined sources
Helixi208 – 2103Combined sources
Helixi215 – 2173Combined sources
Beta strandi224 – 2285Combined sources
Helixi236 – 2438Combined sources
Beta strandi247 – 2548Combined sources
Turni255 – 2573Combined sources
Turni261 – 2633Combined sources
Helixi264 – 2729Combined sources
Beta strandi276 – 2827Combined sources
Turni291 – 2933Combined sources
Helixi297 – 3004Combined sources
Helixi310 – 32011Combined sources
Turni321 – 3233Combined sources
Helixi327 – 33610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP10182.
SMRiP10182. Positions 8-337.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10182.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 337328Asparaginase/glutaminasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1012Substrate bindingBy similarity

Sequence similaritiesi

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

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.

P10182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KEVENQQKLA NVVILATGGT IAGAGASAAN SATYQAAKVG VDKLIAGVPE
60 70 80 90 100
LADLANVRGE QVMQIASESI TNDDLLKLGK RVAELADSND VDGIVITHGT
110 120 130 140 150
DTLEETAYFL DLTLNTDKPI VVVGSMRPGT AMSADGMLNL YNAVAVASNK
160 170 180 190 200
DSRGKGVLVT MNDEIQSGRD VSKSINIKTE AFKSAWGPLG MVVEGKSYWF
210 220 230 240 250
RLPAKRHTVN SEFDIKQISS LPQVDIAYSY GNVTDTAYKA LAQNGAKALI
260 270 280 290 300
HAGTGNGSVS SRLTPALQTL RKTGTQIIRS SHVNQGGFVL RNAEQPDDKN
310 320 330
DWVVAHDLNP EKARILVELA MVKTQDSKEL QRIFWEY
Length:337
Mass (Da):36,200
Last modified:November 1, 1995 - v2
Checksum:i11DEEC467CB1475E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71Q → H AA sequence (PubMed:619999).Curated
Sequence conflicti12 – 121V → R AA sequence (PubMed:619999).Curated

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP10182.
SMRiP10182. Positions 8-337.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.1.38. 5085.

Miscellaneous databases

EvolutionaryTraceiP10182.

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

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Entry informationi

Entry nameiASPQ_PSES7
AccessioniPrimary (citable) accession number: P10182
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1995
Last modified: October 14, 2015
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.