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Entry: A0A2G4EVS9_9CYAN
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ID   A0A2G4EVS9_9CYAN        Unreviewed;       315 AA.
AC   A0A2G4EVS9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Probable aspartoacylase {ECO:0000256|HAMAP-Rule:MF_00704};
DE            EC=3.5.1.15 {ECO:0000256|HAMAP-Rule:MF_00704};
GN   ORFNames=CP500_020435 {ECO:0000313|EMBL:PHX53634.1};
OS   Tychonema bourrellyi FEM_GT703.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Tychonema.
OX   NCBI_TaxID=2040638 {ECO:0000313|EMBL:PHX53634.1, ECO:0000313|Proteomes:UP000226442};
RN   [1] {ECO:0000313|EMBL:PHX53634.1, ECO:0000313|Proteomes:UP000226442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX53634.1,
RC   ECO:0000313|Proteomes:UP000226442};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHX53634.1, ECO:0000313|Proteomes:UP000226442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX53634.1,
RC   ECO:0000313|Proteomes:UP000226442};
RA   Tett A., Armanini F., Asnicar F., Boscaini A., Pasolli E., Zolfo M.,
RA   Donati C., Salmaso N., Segata N.;
RT   "Draft genome sequence of the planktic cyanobacteria Tychonema bourrellyi
RT   isolated from alpine lentic freshwater.";
RL   Submitted (NOV-2017) 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:0000256|HAMAP-Rule:MF_00704};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00704,
CC         ECO:0000256|PIRSR:PIRSR018001-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00704,
CC       ECO:0000256|PIRSR:PIRSR018001-3};
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC       {ECO:0000256|ARBA:ARBA00006173, ECO:0000256|HAMAP-Rule:MF_00704}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHX53634.1}.
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DR   EMBL; NXIB02000169; PHX53634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G4EVS9; -.
DR   OrthoDB; 531770at2; -.
DR   Proteomes; UP000226442; Unassembled WGS sequence.
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   CDD; cd06909; M14_ASPA; 1.
DR   Gene3D; 2.20.25.160; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00704; Aspartoacylase; 1.
DR   InterPro; IPR016708; Aspartoacylase.
DR   InterPro; IPR007036; Aste_AspA.
DR   PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR   PANTHER; PTHR15162:SF7; SUCCINYLGLUTAMATE DESUCCINYLASE; 1.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF018001; Aspartoacylase; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00704};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00704}; Reference proteome {ECO:0000313|Proteomes:UP000226442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00704}.
FT   ACT_SITE        165
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00704,
FT                   ECO:0000256|PIRSR:PIRSR018001-3"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00704,
FT                   ECO:0000256|PIRSR:PIRSR018001-3"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT   BINDING         63..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00704,
FT                   ECO:0000256|PIRSR:PIRSR018001-3"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00704"
SQ   SEQUENCE   315 AA;  35340 MW;  6B0677F9C43C8965 CRC64;
     MNKIKRVAII GGTHGNELIG IYLVNKFDRQ PDLIARSTFQ TMALLANPKA CAIGKRYIDI
     DLNRCFLQQD LENPNLSSYE SERAKEIYHI FSSKNRDDAD LIIDLHTTTS NMGLTFILDS
     QHPFDLQLAT HLTSVYPNFK VLASGTQNQD TSVLRSISKL GFTLEVGPVA QGVLDASLFQ
     QTEALVGTIL DWVEAYNQET IAPVENPLTI YQKVQTIDYP RNESGEIQAM IHPQLQFRDY
     EPLNPGDPMF LTFDGESLFY EGKSTVYPVF INEAAYYEKG ISMYLTQKQI VIGNGEWGIG
     NGELGISNWE LVIGN
//
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