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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121Acyl-ester intermediatePROSITE-ProRule annotation
Binding sitei59 – 591SubstrateBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Glutaminase-asparaginasePRO_0000171087Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
331
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Turni11 – 133Combined sources
Helixi33 – 375Combined sources
Helixi43 – 464Combined sources
Beta strandi47 – 526Combined sources
Helixi59 – 613Combined sources
Helixi64 – 7815Combined sources
Beta strandi85 – 895Combined sources
Helixi92 – 943Combined sources
Helixi95 – 10511Combined sources
Beta strandi112 – 1154Combined sources
Helixi128 – 13912Combined sources
Beta strandi149 – 1535Combined sources
Beta strandi156 – 1594Combined sources
Turni160 – 1623Combined sources
Beta strandi168 – 1703Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi188 – 1914Combined sources
Helixi200 – 2023Combined sources
Turni207 – 2093Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi218 – 2225Combined sources
Helixi230 – 2367Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2488Combined sources
Turni249 – 2513Combined sources
Helixi257 – 26610Combined sources
Beta strandi271 – 2788Combined sources
Turni285 – 2873Combined sources
Helixi291 – 2944Combined sources
Helixi304 – 31411Combined sources
Turni315 – 3173Combined sources
Helixi321 – 3288Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP10172.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 331330Asparaginase/glutaminasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni92 – 932Substrate 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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGXX-ray2.90A1-331[»]
ProteinModelPortaliP10172.
SMRiP10172. Positions 1-331.
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: December 9, 2015
This is version 86 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.