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Protein

N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase

Gene
N/A
Organism
Elizabethkingia miricola (Chryseobacterium miricola)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.

Catalytic activityi

N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei197Nucleophile4 Publications1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Protein family/group databases

MEROPSiT02.007.

Names & Taxonomyi

Protein namesi
Recommended name:
N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase (EC:3.5.1.26)
Alternative name(s):
Aspartylglucosaminidase
Short name:
AGA
Glycosylasparaginase
N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Cleaved into the following 2 chains:
OrganismiElizabethkingia miricola (Chryseobacterium miricola)
Taxonomic identifieri172045 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeElizabethkingia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi197T → A: Abolishes autocatalytic cleavage. 2 Publications1
Mutagenesisi197T → C: Strongly reduced enzyme activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 451 PublicationAdd BLAST45
ChainiPRO_000000234746 – 196Glycosylasparaginase alpha chainAdd BLAST151
ChainiPRO_0000002348197 – 340Glycosylasparaginase beta chainAdd BLAST144

Post-translational modificationi

Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity.

Keywords - PTMi

Autocatalytic cleavage

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.4 Publications

Protein-protein interaction databases

DIPiDIP-61331N.

Structurei

Secondary structure

1340
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 56Combined sources7
Helixi59 – 70Combined sources12
Turni71 – 73Combined sources3
Helixi76 – 89Combined sources14
Helixi91 – 95Combined sources5
Helixi97 – 99Combined sources3
Beta strandi110 – 115Combined sources6
Beta strandi121 – 127Combined sources7
Helixi133 – 143Combined sources11
Beta strandi147 – 150Combined sources4
Helixi151 – 160Combined sources10
Helixi171 – 181Combined sources11
Beta strandi190 – 195Combined sources6
Beta strandi198 – 203Combined sources6
Beta strandi209 – 215Combined sources7
Turni233 – 235Combined sources3
Beta strandi236 – 239Combined sources4
Turni240 – 242Combined sources3
Beta strandi243 – 249Combined sources7
Helixi251 – 257Combined sources7
Helixi259 – 268Combined sources10
Helixi273 – 290Combined sources18
Helixi295 – 297Combined sources3
Beta strandi300 – 306Combined sources7
Beta strandi311 – 317Combined sources7
Beta strandi322 – 326Combined sources5
Beta strandi329 – 333Combined sources5
Beta strandi336 – 338Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYYX-ray2.32A/C46-196[»]
B/D197-340[»]
1P4KX-ray1.90A/C46-340[»]
1P4VX-ray1.90A/C46-340[»]
2GACX-ray2.10A/C46-196[»]
B/D198-340[»]
2GAWX-ray2.20A/C46-196[»]
B/D197-340[»]
2GL9X-ray2.00A/C46-196[»]
B/D197-340[»]
3LJQX-ray1.90A/C46-340[»]
4R4YX-ray2.10A/B46-340[»]
9GAAX-ray2.10A/C46-340[»]
9GACX-ray1.90A/C46-340[»]
9GAFX-ray1.90A/C46-340[»]
ProteinModelPortaliQ47898.
SMRiQ47898.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47898.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni225 – 228Substrate binding4
Regioni248 – 251Substrate binding4

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
IPR019546. TAT_signal_bac_arc.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 1 hit.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01409. TAT_signal_seq. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q47898-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIIYKQQTM NNNRRDFIKK LGIATAAIAI NPLEAKNLLD TSEPKTTNKP
60 70 80 90 100
IVLSTWNFGL HANVEAWKVL SKGGKALDAV EKGVRLVEDD PTERSVGYGG
110 120 130 140 150
RPDRDGRVTL DACIMDENYN IGSVACMEHI KNPISVARAV MEKTPHVMLV
160 170 180 190 200
GDGALEFALS QGFKKENLLT AESEKEWKEW LKTSQYKPIV NIENHDTIGM
210 220 230 240 250
IALDAQGNLS GACTTSGMAY KMHGRVGDSP IIGAGLFVDN EIGAATATGH
260 270 280 290 300
GEEVIRTVGT HLVVELMNQG RTPQQACKEA VERIVKIVNR RGKNLKDIQV
310 320 330 340
GFIALNKKGE YGAYCIQDGF NFAVHDQKGN RLETPGFALK
Length:340
Mass (Da):37,263
Last modified:November 1, 1997 - v1
Checksum:i4C56E5061B4E53D7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08028 Genomic DNA. Translation: AAA68868.1.
PIRiS69194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08028 Genomic DNA. Translation: AAA68868.1.
PIRiS69194.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYYX-ray2.32A/C46-196[»]
B/D197-340[»]
1P4KX-ray1.90A/C46-340[»]
1P4VX-ray1.90A/C46-340[»]
2GACX-ray2.10A/C46-196[»]
B/D198-340[»]
2GAWX-ray2.20A/C46-196[»]
B/D197-340[»]
2GL9X-ray2.00A/C46-196[»]
B/D197-340[»]
3LJQX-ray1.90A/C46-340[»]
4R4YX-ray2.10A/B46-340[»]
9GAAX-ray2.10A/C46-340[»]
9GACX-ray1.90A/C46-340[»]
9GAFX-ray1.90A/C46-340[»]
ProteinModelPortaliQ47898.
SMRiQ47898.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61331N.

Protein family/group databases

MEROPSiT02.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ47898.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
IPR019546. TAT_signal_bac_arc.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 1 hit.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01409. TAT_signal_seq. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiASPG_ELIMR
AccessioniPrimary (citable) accession number: Q47898
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 100 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.