P74383 (ASGX_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoaspartyl peptidase/L-asparaginase
EC=3.4.19.5

Alternative name(s):
Beta-aspartyl-peptidase
Isoaspartyl dipeptidase

Cleaved into the following 2 chains:

1. Isoaspartyl peptidase/L-asparaginase subunit alpha
2. Isoaspartyl peptidase/L-asparaginase subunit beta

Gene names

Ordered Locus Names:

sll0422

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	329 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	Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Probably performs the final step in the degradation of the reserve polymer cyanophycin (depolymerizes the building block L-beta-Asp-Arg). Also has L-asparaginase activity. Ref.1
Catalytic activity	Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers Probable. Ref.1
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. Ref.1
Sequence similarities	Belongs to the Ntn-hydrolase family.
Biophysicochemical properties	Kinetic parameters: Enzyme is inactive on alpha-aspartyl dipeptides. KM=0.66 mM for L-Asn KM=1.0 mM for L-beta-Asp-Ala KM=0.32 mM for L-beta-Asp-Arg KM=1.6 mM for L-beta-Asp-Gly KM=0.33 mM for L-beta-Asp-Leu KM=0.55 mM for L-beta-Asp-Lys KM=0.56 mM for L-beta-Asp-Phe Vmax=1.6 µmol/min/mg enzyme with L-Asn as substrate Vmax=7.3 µmol/min/mg enzyme with L-beta-Asp-Ala as substrate Vmax=21.0 µmol/min/mg enzyme with L-beta-Asp-Arg as substrate Vmax=2.4 µmol/min/mg enzyme with L-beta-Asp-Gly as substrate Vmax=14.7 µmol/min/mg enzyme with L-beta-Asp-Leu as substrate Vmax=29.4 µmol/min/mg enzyme with L-beta-Asp-Lys as substrate Vmax=23.6 µmol/min/mg enzyme with L-beta-Asp-Phe as substrate

Ontologies

Keywords
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-aspartyl-peptidase 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
	Chain	1 – 172	172	Isoaspartyl peptidase/L-asparaginase subunit alpha		PRO_0000184578
	Chain	173 – 329	157	Isoaspartyl peptidase/L-asparaginase subunit beta		PRO_0000329015
Sites
	Active site	173	1	Nucleophile By similarity
	Site	172 – 173	2	Cleavage; by autolysis

Sequences

	Sequence		Length	Mass (Da)
	P74383 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: EBD70950B7F684F5	FASTA	329	34,895
	10 20 30 40 50 60 MTPKLIIHGG ASSLDDKGGL ATVRQSLHQI VAAVYETLTA GGSAMDAVVQ GCELLENEPR 70 80 90 100 110 120 FNAGTGSVLQ SDGQVRMSAS LMDGDRQNFS GVINVSRIKN PIQMAQFLQG QTDRILSDYG 130 140 150 160 170 180 AADLAREMQL PIYDPATDFR IQEWMEERGE DVRKKMARLI ADPTVGIEAR KGTIGVVALD 190 200 210 220 230 240 ANGKIAAGTS TGGKGLERIG RVSDSAMPAG NYATRFAGVS CTGVGEDIIN ECLAAKVVIR 250 260 270 280 290 300 VKDGQNLAQA MAKSITEALE NNTDLGAIAL DHQGHIAWGK TCPVLLAAYH TGTAIGDTLE 310 320 LTDGDHYGNA SILKLQKTVK KIQTKTRGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isoaspartyl dipeptidase activity of plant-type asparaginases." Hejazi M., Piotukh K., Mattow J., Deutzmann R., Volkmer-Engert R., Lockau W. Biochem. J. 364:129-136(2002) [PubMed: 11988085] [Abstract] Cited for: PROTEIN SEQUENCE OF 173-179, FUNCTION, SUBUNIT, AUTOCATALYTIC CLEAVAGE.
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA18480.1.
PIR	S76221.
RefSeq	NP_441802.1. NC_000911.1.
3D structure databases
ProteinModelPortal	P74383.
ModBase	Search...
Protein-protein interaction databases
STRING	P74383.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	952911.
GenomeReviews	Gene locus sll0422 in contig BA000022_GR.
KEGG	syn:sll0422.
NMPDR	fig|1148.1.peg.1903.
PATRIC	23841106. VBISynSp132158_2104.
Phylogenomic databases
eggNOG	COG1446.
HOGENOM	HBG735787.
OMA	IDECLAP.
PhylomeDB	P74383.
ProtClustDB	CLSK893289.
Enzyme and pathway databases
BioCyc	SSP1148:SLL0422-MONOMER.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
KO	K01424.
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASGX_SYNY3

Accession

Primary (citable) accession number: P74383

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program