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Protein

Isoaspartyl peptidase/L-asparaginase

Gene

all3922

Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.

Kineticsi

Enzyme is inactive on alpha-aspartyl dipeptides.
  1. KM=2.0 mM for L-Asn
  2. KM=1.54 mM for L-beta-Asp-Ala
  3. KM=0.27 mM for L-beta-Asp-Arg
  4. KM=0.52 mM for L-beta-Asp-Gly
  5. KM=0.26 mM for L-beta-Asp-Leu
  6. KM=0.53 mM for L-beta-Asp-Lys
  7. KM=0.68 mM for L-beta-Asp-Phe
  1. Vmax=2.2 µmol/min/mg enzyme with L-Asn as substrate
  2. Vmax=12.3 µmol/min/mg enzyme with L-beta-Asp-Ala as substrate
  3. Vmax=5.7 µmol/min/mg enzyme with L-beta-Asp-Arg as substrate
  4. Vmax=2.7 µmol/min/mg enzyme with L-beta-Asp-Gly as substrate
  5. Vmax=4.5 µmol/min/mg enzyme with L-beta-Asp-Leu as substrate
  6. Vmax=22.2 µmol/min/mg enzyme with L-beta-Asp-Lys as substrate
  7. Vmax=20.1 µmol/min/mg enzyme with L-beta-Asp-Phe as substrate

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei180NucleophileBy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Protease

Enzyme and pathway databases

SABIO-RKiQ8YQB1.

Protein family/group databases

MEROPSiT02.002.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Ordered Locus Names:all3922
OrganismiNostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
Proteomesi
  • UP000002483 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003440631 – 179Isoaspartyl peptidase/L-asparaginase subunit alphaAdd BLAST179
ChainiPRO_0000344064180 – 318Isoaspartyl peptidase/L-asparaginase subunit betaAdd BLAST139

Post-translational modificationi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei179 – 180Cleavage; by autolysis2

Keywords - PTMi

Autocatalytic cleavage

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.1 Publication

Protein-protein interaction databases

STRINGi103690.all3922.

Structurei

3D structure databases

ProteinModelPortaliQ8YQB1.
SMRiQ8YQB1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni208 – 211Substrate bindingBy similarity4
Regioni229 – 232Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Phylogenomic databases

eggNOGiENOG4105D44. Bacteria.
COG1446. LUCA.
HOGENOMiHOG000174613.
KOiK01424.
OMAiSDGQIRM.
OrthoDBiPOG091H0I7Z.

Family and domain databases

InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
PANTHERiPTHR10188. PTHR10188. 1 hit.
PfamiView protein in Pfam
PF01112. Asparaginase_2. 1 hit.
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8YQB1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSQVQPKLI IHGGAGSSLH GKGGLEAVRQ TLHAVVEEVY ALLLSGVNAS
60 70 80 90 100
VAVVRGCQLL EDEPRFNAGT GSVLQSDGQI RMSASIMDGA LGRFSGVINV
110 120 130 140 150
SRVKNPIELA QFLQNSPDRV LSDYGSAELA REMQIPSYNA LTELRLQEWI
160 170 180 190 200
QERQDNFKRT MAGVIAEPEL LETSNAGRGT IGVVALDTYG KLAVGTSTGG
210 220 230 240 250
KGFERIGRVS DSAMPAGNYA TSYAAVSCTG IGEDIIDECL APKIVIRVTD
260 270 280 290 300
GLSLQDSMQR SFAEAHDNKR DFGAIALDAN GAIAWGKTCD IILAAFHDGE
310
KIGDTLELAV GTQVGSIS
Length:318
Mass (Da):33,638
Last modified:March 1, 2002 - v1
Checksum:iBB922A9D87C7B557
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000019 Genomic DNA. Translation: BAB75621.1.
PIRiAC2296.
RefSeqiWP_010998063.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB75621; BAB75621; BAB75621.
KEGGiana:all3922.

Similar proteinsi

Entry informationi

Entry nameiASGX_NOSS1
AccessioniPrimary (citable) accession number: Q8YQB1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: March 1, 2002
Last modified: June 7, 2017
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families