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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)DescriptionActionsGraphical viewLength
Active sitei20Acyl-ester intermediatePROSITE-ProRule annotation1 Publication1
Binding sitei67SubstrateBy similarity1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001710891 – 337Glutaminase-asparaginaseAdd BLAST337

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 19Combined sources9
Helixi20 – 22Combined sources3
Beta strandi26 – 29Combined sources4
Beta strandi31 – 37Combined sources7
Helixi41 – 46Combined sources6
Helixi51 – 54Combined sources4
Beta strandi56 – 65Combined sources10
Helixi67 – 69Combined sources3
Helixi72 – 87Combined sources16
Beta strandi92 – 97Combined sources6
Helixi100 – 102Combined sources3
Helixi103 – 113Combined sources11
Beta strandi120 – 123Combined sources4
Helixi136 – 147Combined sources12
Helixi150 – 152Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi164 – 167Combined sources4
Turni168 – 170Combined sources3
Beta strandi171 – 173Combined sources3
Beta strandi175 – 178Combined sources4
Beta strandi182 – 184Combined sources3
Beta strandi189 – 193Combined sources5
Beta strandi196 – 199Combined sources4
Beta strandi201 – 203Combined sources3
Helixi208 – 210Combined sources3
Helixi215 – 217Combined sources3
Beta strandi224 – 228Combined sources5
Helixi236 – 243Combined sources8
Beta strandi247 – 254Combined sources8
Turni255 – 257Combined sources3
Turni261 – 263Combined sources3
Helixi264 – 272Combined sources9
Beta strandi276 – 282Combined sources7
Turni291 – 293Combined sources3
Helixi297 – 300Combined sources4
Helixi310 – 320Combined sources11
Turni321 – 323Combined sources3
Helixi327 – 336Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10182.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 337Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST328

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni100 – 101Substrate bindingBy similarity2

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)DescriptionActionsGraphical viewLength
Sequence conflicti7Q → H AA sequence (PubMed:619999).Curated1
Sequence conflicti12V → R AA sequence (PubMed:619999).Curated1

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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...

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: November 2, 2016
This is version 88 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.