ID   ASPA_SYNS9              Reviewed;         303 AA.
AC   Q3AV13;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Probable aspartoacylase {ECO:0000255|HAMAP-Rule:MF_00704};
DE            EC=3.5.1.15 {ECO:0000255|HAMAP-Rule:MF_00704};
GN   OrderedLocusNames=Syncc9902_1819;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate;
CC         Xref=Rhea:RHEA:10872, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58497; EC=3.5.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00704};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00704};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00704};
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00704}.
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DR   EMBL; CP000097; ABB26776.1; -; Genomic_DNA.
DR   RefSeq; WP_011360580.1; NC_007513.1.
DR   AlphaFoldDB; Q3AV13; -.
DR   SMR; Q3AV13; -.
DR   STRING; 316279.Syncc9902_1819; -.
DR   EnsemblBacteria; ABB26776; ABB26776; Syncc9902_1819.
DR   KEGG; sye:Syncc9902_1819; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_083292_0_0_3; -.
DR   OMA; THGNEIN; -.
DR   OrthoDB; 632656at2; -.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0019807; F:aspartoacylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00704; Aspartoacylase; 1.
DR   InterPro; IPR016708; Aspartoacylase.
DR   InterPro; IPR007036; Aste_AspA.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF018001; Aspartoacylase; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..303
FT                   /note="Probable aspartoacylase"
FT                   /id="PRO_1000045517"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         62..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
SQ   SEQUENCE   303 AA;  33573 MW;  9C33AD5887338819 CRC64;
     MAASDVLVVA GTHGNELNAP WLLEQWNRQP DLINSAGLSI QRLVGNPQAK AAMRRYVDRD
     LNRSFRVDLL EQSGGDLEMR RARELLGRYG PRGDEPCSVV LDLHSTTAAM GCSLVLYGRR
     PADLALAALV QSALGLPIYL HESDSAQTGF LVERWPCGLV VEVGPVPQGV LEARIVRQTR
     LAIEACFEAL ASVRSGVVRL PRQVVVHRHL GSCDVPRGES DQPQALVHQR LQGRDWVPFK
     PLDAIFEAAD GSTVETPQME HQSIPVFINE AAYAEKHIAF SLTRREVWTM EPQWLDHLSE
     LLS