ID   ASPA_SYNY3              Reviewed;         288 AA.
AC   P73211;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=slr1705;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17238.1; -; Genomic_DNA.
DR   PIR; S75324; S75324.
DR   AlphaFoldDB; P73211; -.
DR   SMR; P73211; -.
DR   IntAct; P73211; 1.
DR   STRING; 1148.1652315; -.
DR   PaxDb; P73211; -.
DR   EnsemblBacteria; BAA17238; BAA17238; BAA17238.
DR   KEGG; syn:slr1705; -.
DR   eggNOG; COG2988; Bacteria.
DR   InParanoid; P73211; -.
DR   OMA; THGNEIN; -.
DR   PhylomeDB; P73211; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019807; F:aspartoacylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
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..288
FT                   /note="Probable aspartoacylase"
FT                   /id="PRO_0000216882"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         65..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
SQ   SEQUENCE   288 AA;  32198 MW;  9312F1C762AD7D76 CRC64;
     MVNSAVRSLA IVGGVHGNER TGVEVVRRWQ QKDFARYFPA LKCHYFLANP RAIAANRRYI
     NQDLNRCFRP QDRKNPYLMG YEQLRARQLA HQISLAGIDF IVDLHTTTAA MGTTLILNCP
     HPLLLNLAAY LSAQDEEIRV LQYSPQKDLP YIRGLCELGL TIELGPVPQG VYDPTAIAKT
     QRTLARILAY LQASTSGNVP AADNCTVYQQ IDTIDYPRDE QGQIVAEIAP HIRDYQAIKP
     GTPLFYHRRG NVTPYQGAAT VYPVFIGEAA YVEKGIAMAL TQRKTIAI