Reviewed, UniProtKB/Swiss-Prot Q5JHT1 (ASGX_PYRKO)

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:

TK2246

Organism

Pyrococcus kodakaraensis (Thermococcus kodakaraensis) [Complete proteome] [HAMAP]

Taxonomic identifier

311400 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length	306 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 – 175	175	Putative L-asparaginase subunit alpha		PRO_0000184582
	Chain	176 – 306	131	Putative L-asparaginase subunit beta		PRO_0000329019
Sites
	Active site	176	1	Nucleophile By similarity
	Site	174 – 175	2	Cleavage; by autolysis Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5JHT1-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 0290276B98DDC5F9	FASTA	306	32,642
	10 20 30 40 50 60 MAAIIVHGGA GTIRKEERIP KVIEGVREAV LAGWRELKRG SALDAVEEAV KALEDNPIFN 70 80 90 100 110 120 AGTGSVLTLD GKVEMDAAIM RGKTLDAGAV AGIWGVKNPI SVARKVMEKT DHVLLIGEGA 130 140 150 160 170 180 VKFARLLGFE EYDPITEERL KQWEELRKKL IEKGETKHWK KLNELIKEYP EVLRSTVGAV 190 200 210 220 230 240 AFDGEEVVAG TSTGGVFLKM FGRVGDTPII GGGTYANEVA GASCTGLGEV AIKLALAKSA 250 260 270 280 290 300 ADFVRLGMDA QTASEAAISL ATKYFGPDTM GIIMVDAKGN VGFAKNTKHM SYAFMKDGMD EPEAGV

References

[1]

"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes." Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T. Genome Res. 15:352-363(2005) [PubMed: 15710748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KOD1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006878 Genomic DNA. Translation: BAD86435.1.
RefSeq	YP_184659.1.
3D structure databases
SMR	Q5JHT1. Positions 2-149, 3-304.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5JHT1.
Genome annotation databases
GeneID	3234510.
GenomeReviews	Gene locus TK2246 in contig AP006878_GR.
KEGG	tko:TK2246.
NMPDR	fig|69014.3.peg.2246.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG09766.
HOGENOM	HBG735787.
OMA	NKQVGRV.
PhylomeDB	Q5JHT1.
Enzyme and pathway databases
BioCyc	TKOD69014:TK2246-MONOMER.
BRENDA	3.5.1.1. 192130.
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_PYRKO

Accession

Primary (citable) accession number: Q5JHT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	February 15, 2005
Last modified:	January 19, 2010
This is version 29 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)