Reviewed, UniProtKB/Swiss-Prot Q9V262 (ASGX_PYRAB)

Names and origin

Protein names

Recommended name:
    Putative L-asparaginase
    EC=3.5.1.1
Alternative name(s):
    L-asparagine amidohydrolase
Cleaved into the following 2 chains:
    1- Recommended name:
            Putative L-asparaginase subunit alpha
    2- Recommended name:
            Putative L-asparaginase subunit beta

Gene names

Ordered Locus Names:	PYRAB02120
ORF Names:	PAB0145

Organism

Pyrococcus abyssi [Complete proteome] [HAMAP]

Taxonomic identifier

29292 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Post-translational modification	Autocleaved. Generates the alpha and beta subunits. The N-terminal residue of the beta subunit is thought to be responsible for the nucleophile hydrolase activity Potential.
Sequence similarities	Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	asparaginase activity Inferred from electronic annotation. Source: EC 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
	Chain	1 – 174	174	Putative L-asparaginase subunit alpha		PRO_0000184579
	Chain	175 – 305	131	Putative L-asparaginase subunit beta		PRO_0000329016
Sites
	Active site	175	1	Nucleophile By similarity
	Site	174 – 175	2	Cleavage; by autolysis Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9V262-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5B2A1DE8F6FB2F7B	FASTA	305	32,591
	10 20 30 40 50 60 MVAIIVHGGA GTIRKEERIP KVLEGVREAV LAGWKELKKG SALDAVEEAI KVLEDNPIFN 70 80 90 100 110 120 AGTGSVLTID GKVEMDAAIM RGKTLEAGAV AGIWGVKNPI SVARKVMEKT DHVLLVGEGA 130 140 150 160 170 180 VKFARIMGFP EYDPTTEERR KQWQELKEKL MKGEVRHWKK LGELIKEHPE VLRSTVGAVA 190 200 210 220 230 240 FDGEEVVAGT STGGVFLKMF GRVGDTPIIG AGTYANEVAG ASCTGLGEVA IKLALAKTAT 250 260 270 280 290 300 DFVRLGLDAQ AASEAAIELA TKHFGKDTMG IIMVDSRGNV GFAKNTKHMS YAFMKEGMNE PEAGV

References

[1]

"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ248283 Genomic DNA. Translation: CAB49136.1.
PIR	A75211.
RefSeq	NP_125905.1.
3D structure databases
HSSP	HSSP built from PDB template 9GAF based on UniProtKB Q47898.
ModBase	Search...
Protein family/group databases
MEROPS	T02.002.
Genome annotation databases
GeneID	1495101.
GenomeReviews	Gene locus PYRAB02120 in contig AL096836_GR.
KEGG	pab:PAB0145.
NMPDR	fig|272844.1.peg.225.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9V262.
OMA	MVAIIVH.
Enzyme and pathway databases
BioCyc	PABY272844:PAB0145-MON.
BRENDA	3.5.1.1. 262861.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASGX_PYRAB

Accession

Primary (citable) accession number: Q9V262

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)