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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei197 – 1971Nucleophile4 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi197 – 1971T → A: Abolishes autocatalytic cleavage. 2 Publications
Mutagenesisi197 – 1971T → C: Strongly reduced enzyme activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 45451 PublicationAdd
BLAST
Chaini46 – 196151Glycosylasparaginase alpha chainPRO_0000002347Add
BLAST
Chaini197 – 340144Glycosylasparaginase beta chainPRO_0000002348Add
BLAST

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

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 567Combined sources
Helixi59 – 7012Combined sources
Turni71 – 733Combined sources
Helixi76 – 8914Combined sources
Helixi91 – 955Combined sources
Helixi97 – 993Combined sources
Beta strandi110 – 1156Combined sources
Beta strandi121 – 1277Combined sources
Helixi133 – 14311Combined sources
Beta strandi147 – 1504Combined sources
Helixi151 – 16010Combined sources
Helixi171 – 18111Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi198 – 2036Combined sources
Beta strandi209 – 2157Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2394Combined sources
Turni240 – 2423Combined sources
Beta strandi243 – 2497Combined sources
Helixi251 – 2577Combined sources
Helixi259 – 26810Combined sources
Helixi273 – 29018Combined sources
Helixi295 – 2973Combined sources
Beta strandi300 – 3067Combined sources
Beta strandi311 – 3177Combined sources
Beta strandi322 – 3265Combined sources
Beta strandi329 – 3335Combined sources
Beta strandi336 – 3383Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 46-340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ47898.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 2284Substrate binding
Regioni248 – 2514Substrate binding

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
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. Positions 46-340.
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...

Publicationsi

  1. "Molecular cloning and sequence analysis of Flavobacterium meningosepticum glycosylasparaginase: a single gene encodes the alpha and beta subunits."
    Tarentino A.L., Quinones G., Hauer C.R., Changchien L.-M., Plummer T.H. Jr.
    Arch. Biochem. Biophys. 316:399-406(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 33958.
  2. "The first demonstration of a procaryotic glycosylasparaginase."
    Tarentino A.L., Plummer T.H. Jr.
    Biochem. Biophys. Res. Commun. 197:179-186(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 46-59 AND 197-211.
  3. "Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum."
    Xuan J., Tarentino A.L., Grimwood B.G., Plummer T.H. Jr., Cui T., Guan C., van Roey P.
    Protein Sci. 7:774-781(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).
  4. "Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis."
    Guo H.C., Xu Q., Buckley D., Guan C.
    J. Biol. Chem. 273:20205-20212(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), ACTIVE SITE, SUBUNIT.
  5. "Structural insights into the mechanism of intramolecular proteolysis."
    Xu Q., Buckley D., Guan C., Guo H.C.
    Cell 98:651-661(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 47-340, ACTIVE SITE, CLEAVAGE BY AUTOCATALYSIS, MUTAGENESIS OF THR-197, SUBUNIT.
  6. "Crystallographic snapshot of a productive glycosylasparaginase-substrate complex."
    Wang Y., Guo H.C.
    J. Mol. Biol. 366:82-92(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT CYS-197 IN COMPLEX WITH SUBSTRATE, ACTIVE SITE, CLEAVAGE BY AUTOCATALYSIS, SUBUNIT, MUTAGENESIS OF THR-197.
  7. "Crystallographic snapshot of glycosylasparaginase precursor poised for autoprocessing."
    Wang Y., Guo H.C.
    J. Mol. Biol. 403:120-130(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 46-340 OF MUTANT CYS-197, ACTIVE SITE, CLEAVAGE BY AUTOCATALYSIS, SUBUNIT.

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: December 9, 2015
This is version 98 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.