ID   ASPA_TRIV2              Reviewed;         293 AA.
AC   Q3MC79;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Ava_1785;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA21407.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MC79; -.
DR   SMR; Q3MC79; -.
DR   STRING; 240292.Ava_1785; -.
DR   EnsemblBacteria; ABA21407; ABA21407; Ava_1785.
DR   KEGG; ava:Ava_1785; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_083292_0_0_3; -.
DR   OMA; THGNEIN; -.
DR   Proteomes; UP000002533; 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; Zinc.
FT   CHAIN           1..293
FT                   /note="Probable aspartoacylase"
FT                   /id="PRO_1000045515"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         63..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
SQ   SEQUENCE   293 AA;  32817 MW;  1D0E44017204E397 CRC64;
     MNKINRVAII GGTHGNEFTG AFLVKKFQQF PEVIQKPSFE TLTILGNPKA FEAGKRYIEK
     DLNRCFLTES LQNPNLSSYE DIRAKQIAGV LGEENQPKVD VVIDLHSTTA NMGLSIILGN
     QDPFLLKLCA YLSEINPLVK VCYTIPEKGS NFLRSLNKLG FVIEVGAVAQ GVLNAELFQK
     TEQLIYTILD YVEKYNQGNI PKINNLLSLY KFTGTIDYPR NGNGDIQAMI HPDIQFRDYA
     PLNPGDPLFL TLDGKAIAYE GTSIVYPIFI NEAAYYEKGI AMLFTEKQLI NFD