ASGX_DICDI
ID ASGX_DICDI Reviewed; 346 AA.
AC Q54WW4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative isoaspartyl peptidase/L-asparaginase;
DE EC=3.4.19.5;
DE EC=3.5.1.1;
DE AltName: Full=Beta-aspartyl-peptidase;
DE AltName: Full=Isoaspartyl dipeptidase;
DE AltName: Full=L-asparagine amidohydrolase;
DE Contains:
DE RecName: Full=Putative isoaspartyl peptidase/L-asparaginase alpha chain;
DE Contains:
DE RecName: Full=Putative isoaspartyl peptidase/L-asparaginase beta chain;
DE Flags: Precursor;
GN ORFNames=DDB_G0279357;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC Does not have aspartylglucosaminidase activity and is inactive toward
CC GlcNAc-L-Asn. Likewise, has no activity toward glutamine (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC autocleavage. {ECO:0000250}.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolases family. {ECO:0000305}.
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DR EMBL; AAFI02000030; EAL67827.1; -; Genomic_DNA.
DR RefSeq; XP_641813.1; XM_636721.1.
DR AlphaFoldDB; Q54WW4; -.
DR SMR; Q54WW4; -.
DR STRING; 44689.DDB0230992; -.
DR PaxDb; Q54WW4; -.
DR EnsemblProtists; EAL67827; EAL67827; DDB_G0279357.
DR GeneID; 8622009; -.
DR KEGG; ddi:DDB_G0279357; -.
DR dictyBase; DDB_G0279357; -.
DR eggNOG; KOG1592; Eukaryota.
DR HOGENOM; CLU_021603_1_0_1; -.
DR InParanoid; Q54WW4; -.
DR OMA; YSRMRWK; -.
DR PhylomeDB; Q54WW4; -.
DR PRO; PR:Q54WW4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; IBA:GO_Central.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..206
FT /note="Putative isoaspartyl peptidase/L-asparaginase alpha
FT chain"
FT /id="PRO_0000329020"
FT CHAIN 207..346
FT /note="Putative isoaspartyl peptidase/L-asparaginase beta
FT chain"
FT /id="PRO_0000329021"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 235..238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 257..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 206..207
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 37216 MW; C25D190A81273F09 CRC64;
MNKKSVLVIH GGAGVISKST ISKEREEIFL NSLKNILLAG KIILKQGGTS LDVVQEAVRL
LEEDPIYNAG KGSVFTELGT NEMDAAIMDG TNLKAGAVGG VSIIRNPIIA ARAVMEHTNH
CLLVGKGAEE FAKSKNLEIV EPSFFFTQNR YDQLLRAKDE KKLILDHDGE NLLEKEKEKE
KNNETSTTTT TISVGVDPID PKYKMGTVGA VCLDSFGNLA AATSTGGMTN KMHGRVGDTP
IIGAGVYANK NVAVSSTGTG EAFMRTVAAF DIAAMMEYGS LSLKDASNKV VMEKLITVGD
GGVICVDKYG NVEMPFNTEG MYRGYVIIDN NCENDQNDII NVSIYK
