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Protein

Glutaminase-asparaginase

Gene

ansB

Organism
Acinetobacter glutaminasificans
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei12Acyl-ester intermediatePROSITE-ProRule annotation1
Binding sitei59SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

SABIO-RKP10172.

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
Gene namesi
Name:ansB
OrganismiAcinetobacter glutaminasificans
Taxonomic identifieri474 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001710871 – 331Glutaminase-asparaginaseAdd BLAST331

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Turni11 – 13Combined sources3
Helixi33 – 37Combined sources5
Helixi43 – 46Combined sources4
Beta strandi47 – 52Combined sources6
Helixi59 – 61Combined sources3
Helixi64 – 78Combined sources15
Beta strandi85 – 89Combined sources5
Helixi92 – 94Combined sources3
Helixi95 – 105Combined sources11
Beta strandi112 – 115Combined sources4
Helixi128 – 139Combined sources12
Beta strandi149 – 153Combined sources5
Beta strandi156 – 159Combined sources4
Turni160 – 162Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi181 – 185Combined sources5
Beta strandi188 – 191Combined sources4
Helixi200 – 202Combined sources3
Turni207 – 209Combined sources3
Beta strandi212 – 214Combined sources3
Beta strandi218 – 222Combined sources5
Helixi230 – 236Combined sources7
Turni237 – 239Combined sources3
Beta strandi241 – 248Combined sources8
Turni249 – 251Combined sources3
Helixi257 – 266Combined sources10
Beta strandi271 – 278Combined sources8
Turni285 – 287Combined sources3
Helixi291 – 294Combined sources4
Helixi304 – 314Combined sources11
Turni315 – 317Combined sources3
Helixi321 – 328Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGXX-ray2.90A1-331[»]
ProteinModelPortaliP10172.
SMRiP10172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10172.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 331Asparaginase/glutaminasePROSITE-ProRule annotationAdd BLAST330

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni92 – 93Substrate 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.

P10172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KNNVVIVATG GTIAGAGASS TNSATYSAAK VPVDALIKAV PQVNDLANIT
60 70 80 90 100
GIQALQVASE SITDKELLSL ARQVNDLVKK PSVNGVVITH GTDTMEETAF
110 120 130 140 150
FLNLVVHTDK PIVLVGSMRP STALSADGPL NLYSAVALAS SNEAKNKGVM
160 170 180 190 200
VLMNDSIFAA RDVTKGINIH THAFVSQWGA LGTLVEGKPY WFRSSVKKHT
210 220 230 240 250
NNSEFNIEKI QGDALPGVQI VYGSDNMMPD AYQAFAKAGV KAIIHAGTGN
260 270 280 290 300
GSMANYLVPE VRKLHDEQGL QIVRSSRVAQ GFVLRNAEQP DDKYGWIAAH
310 320 330
DLNPQKARLL MALALTKTND AKEIQNMFWN Y
Length:331
Mass (Da):35,485
Last modified:July 1, 1989 - v1
Checksum:i70F1BF823E9B0D31
GO

Sequence databases

PIRiA28063.

Cross-referencesi

Sequence databases

PIRiA28063.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGXX-ray2.90A1-331[»]
ProteinModelPortaliP10172.
SMRiP10172.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP10172.

Miscellaneous databases

EvolutionaryTraceiP10172.

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_ACIGL
AccessioniPrimary (citable) accession number: P10172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 88 of the entry and version 1 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.