ID   ASPA_PROMM              Reviewed;         304 AA.
AC   Q7V5L6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Probable aspartoacylase;
DE            EC=3.5.1.15;
GN   OrderedLocusNames=PMT_1537;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX548175; CAE21712.1; -; Genomic_DNA.
DR   RefSeq; WP_011130904.1; NC_005071.1.
DR   AlphaFoldDB; Q7V5L6; -.
DR   SMR; Q7V5L6; -.
DR   STRING; 74547.PMT_1537; -.
DR   EnsemblBacteria; CAE21712; CAE21712; PMT_1537.
DR   KEGG; pmt:PMT_1537; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_083292_0_0_3; -.
DR   OMA; THGNEIN; -.
DR   OrthoDB; 632656at2; -.
DR   Proteomes; UP000001423; 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..304
FT                   /note="Probable aspartoacylase"
FT                   /id="PRO_0000216879"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   304 AA;  33250 MW;  0A9465E44589380C CRC64;
     MSGLQVLLVA GTHGNEINGP WLLDQWSQTP ELINTHGVGV VPVIGNPEAL ALGRRYLDCD
     LNRSFRLDLL RSPSILDREV VRAKQLLSFF GPEGSTPCQI VIDLHSTTSA MGSTLVVYGR
     RSVDLALAAL IQARLGLPIY LHDGDDDQQG FLVERWPCGL VIEIGPVPQG LLKARIIEQT
     RLAVQACLEA LSSVASGSPT YPDEFVVHSH LGSLDLPRDA LGQPAACVHP SLQGRDWQPL
     QMGAPLFLWP DGEVFRFEGR DSPIPVFINE AAYVEKHIAM SLTCREVCPL PEQWQGALQQ
     LVDC