Q47898 (ASPG_ELIMR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	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: Glycosylasparaginase alpha chain Glycosylasparaginase beta chain
Organism	Elizabethkingia miricola (Chryseobacterium miricola)
Taxonomic identifier	172045 [NCBI]
Taxonomic lineage	Bacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 45

45

Ref.2

Chain

46 – 196

151

Glycosylasparaginase alpha chain

PRO_0000002347

Chain

197 – 340

144

Glycosylasparaginase beta chain

PRO_0000002348

Sites

Active site

197

1

Nucleophile

Secondary structure

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340

Helix Strand Turn

Details...

Beta strand

50 – 56

7

Helix

59 – 70

12

Turn

71 – 73

3

Helix

76 – 88

13

Beta strand

110 – 115

6

Beta strand

121 – 127

7

Helix

133 – 143

11

Beta strand

147 – 150

4

Helix

151 – 160

10

Helix

171 – 183

13

Beta strand

190 – 195

6

Beta strand

198 – 203

6

Beta strand

209 – 215

7

Turn

232 – 234

3

Beta strand

235 – 239

5

Turn

240 – 242

3

Beta strand

243 – 249

7

Helix

251 – 257

7

Helix

259 – 269

11

Helix

273 – 290

18

Helix

295 – 297

3

Beta strand

300 – 306

7

Beta strand

311 – 317

7

Beta strand

322 – 326

5

Beta strand

329 – 333

5

Sequences

	Sequence		Length	Mass (Da)
	Q47898 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 4C56E5061B4E53D7	FASTA	340	37,263
	10 20 30 40 50 60 MRIIYKQQTM NNNRRDFIKK LGIATAAIAI NPLEAKNLLD TSEPKTTNKP IVLSTWNFGL 70 80 90 100 110 120 HANVEAWKVL SKGGKALDAV EKGVRLVEDD PTERSVGYGG RPDRDGRVTL DACIMDENYN 130 140 150 160 170 180 IGSVACMEHI KNPISVARAV MEKTPHVMLV GDGALEFALS QGFKKENLLT AESEKEWKEW 190 200 210 220 230 240 LKTSQYKPIV NIENHDTIGM IALDAQGNLS GACTTSGMAY KMHGRVGDSP IIGAGLFVDN 250 260 270 280 290 300 EIGAATATGH GEEVIRTVGT HLVVELMNQG RTPQQACKEA VERIVKIVNR RGKNLKDIQV 310 320 330 340 GFIALNKKGE YGAYCIQDGF NFAVHDQKGN RLETPGFALK

References

[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: 7840643] [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: 8250923] [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: 9541410] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U08028 Genomic DNA. Translation: AAA68868.1.

PIR

S69194.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AYY	X-ray	2.32	A/C	46-196	[»]
			B/D	197-340	[»]
1P4K	X-ray	1.90	A/C	46-340	[»]
1P4V	X-ray	1.90	A/C	46-340	[»]
2GAC	X-ray	2.10	A/C	46-196	[»]
			B/D	198-340	[»]
2GAW	X-ray	2.20	A/C	46-196	[»]
			B/D	197-340	[»]
2GL9	X-ray	2.00	A/C	46-196	[»]
			B/D	198-340	[»]
3LJQ	X-ray	1.90	A/C	46-340	[»]
9GAA	X-ray	2.10	A/C	46-340	[»]
9GAC	X-ray	1.90	A/C	46-340	[»]
9GAF	X-ray	1.90	A/C	47-340	[»]

ProteinModelPortal

Q47898.

SMR

Q47898. Positions 46-340.

ModBase

Search...

Protein family/group databases

MEROPS

T02.007.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000246. Peptidase_T2.
IPR019546. TAT_signal_bac_arc.
[Graphical view]

PANTHER

PTHR10188. Peptidase_T2. 1 hit.

Pfam

PF01112. Asparaginase_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01409. TAT_signal_seq. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ASPG_ELIMR

Accession

Primary (citable) accession number: Q47898

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program