ID   ASPA_PROMT              Reviewed;         305 AA.
AC   Q46HE9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-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=PMN2A_1591;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ59079.1; -; Genomic_DNA.
DR   RefSeq; WP_011294224.1; NC_007335.2.
DR   AlphaFoldDB; Q46HE9; -.
DR   SMR; Q46HE9; -.
DR   STRING; 59920.PMN2A_1591; -.
DR   EnsemblBacteria; AAZ59079; AAZ59079; PMN2A_1591.
DR   KEGG; pmn:PMN2A_1591; -.
DR   HOGENOM; CLU_083292_0_0_3; -.
DR   OMA; THGNEIN; -.
DR   OrthoDB; 632656at2; -.
DR   PhylomeDB; Q46HE9; -.
DR   Proteomes; UP000002535; 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..305
FT                   /note="Probable aspartoacylase"
FT                   /id="PRO_1000147942"
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         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         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
SQ   SEQUENCE   305 AA;  35130 MW;  572B88497A72E305 CRC64;
     MKQLQVLLVA GTHGNEINGI WLFDEWKKSS FLINTHGIKT FKVIGNPEAK KAGKRYIHHD
     LNRSFKEESF IKINPLNCER TRASELVNLY GEAGENPCQI ALDFHTTTAS MGSCIVVYGR
     RDADLALASL IQNQLGLPVY LHESDQKQTG FLVESWPCGL VVEIGPIGQG LLNSRIISQT
     KLILETLMEQ IHEVKNLNLF FPNKLIIHRH IKSIDFPRDE EGNIDGYVHS LRQSKDWQEL
     KKNDELFCKL NGEIIRFEED EPYIPVFINE AAYVEKNIAM SFTKRELWNF KKEWKQALID
     LIHQK