B4QHB1 (ASPG1_DROSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase GD10667
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:

1. Glycosylasparaginase alpha chain
2. Glycosylasparaginase beta chain

Gene names

ORF Names:

GD10667

Organism

Drosophila simulans (Fruit fly) [Complete proteome]

Taxonomic identifier

7240 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins By similarity. UniProtKB P20933
Catalytic activity	N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate. UniProtKB P20933
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity. UniProtKB P20933
Post-translational modification	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 By similarity.
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein deglycosylation Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	lysosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from sequence or structural similarity. Source: UniProtKB peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 242	219	Glycosylasparaginase alpha chain UniProtKB P20933		PRO_0000384137
	Chain	243 – 393	151	Glycosylasparaginase beta chain UniProtKB P20933		PRO_0000384138
Regions
	Region	271 – 274	4	Substrate binding By similarity
	Region	294 – 297	4	Substrate binding By similarity
Sites
	Active site	243	1	Nucleophile By similarity UniProtKB P20933
Amino acid modifications
	Disulfide bond	97 ↔ 102		By similarity UniProtKB P20933
	Disulfide bond	196 ↔ 212		By similarity UniProtKB P20933
	Disulfide bond	354 ↔ 381		By similarity UniProtKB P20933

Sequences

	Sequence		Length	Mass (Da)
	B4QHB1 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 76F0AF4EE97CE4C3	FASTA	393	42,219
	10 20 30 40 50 60 MRTHLRASLW VLCLASMAFS ILAAVNTSPK PTLASAFSGK AGTPAVKANK TTGELLPMVI 70 80 90 100 110 120 NTWNFTAANV LAWRILKQSK GGLRQTRNAV VEGCSKCEKL QCDRTVGYGG SPDELGETTL 130 140 150 160 170 180 DAMVMDGATM DVGAVAGLRR IKDAIKVARH VLEHTQHTML VGDAASAFAN AMGFESESLV 190 200 210 220 230 240 TPESKDMWLQ WTAENCQPNF WKNVHPDPKV SCGPYKPRPT PLTRWKEDRA RNEYEIGRKN 250 260 270 280 290 300 HDTIGMIAID VENNIHAGTS TNGARHKIPG RVGDSPIPGA GAYADNEVGA AVATGDGDVM 310 320 330 340 350 360 MRFLPSLLAV EAMRAGKPPA EAAQGGLRRI LKHHKDFMGA LIAVDRLGNY GAACYGLEEF 370 380 390 PFMVSSPAGA DRPTRLETVK CIAGQDKVNI VAL

References

[1]	"Evolution of genes and genomes on the Drosophila phylogeny." Drosophila 12 genomes consortium Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CM000362 Genomic DNA. Translation: EDX06365.1.
RefSeq	XP_002080780.1. XM_002080744.1.
UniGene	Dsi.10460.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T02.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0210577; FBpp0209069; FBgn0182434.
GeneID	6733734.
KEGG	dsi:Dsim_GD10667.
Organism-specific databases
FlyBase	FBgn0182434. Dsim\GD10667.
Phylogenomic databases
KO	K01444.
OrthoDB	EOG44MW7V.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. PTHR10188. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASPG1_DROSI

Accession

Primary (citable) accession number: B4QHB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	September 23, 2008
Last modified:	February 6, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project