ID   ASPA_PROMA              Reviewed;         307 AA.
AC   P72208;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 102.
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=Pro_0251;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=9255521; DOI=10.3109/10425179709034049;
RA   Hess W.R.;
RT   "Localization of an open reading frame with homology to human
RT   aspartoacylase upstream from psbA in the prokaryote Prochlorococcus marinus
RT   CCMP 1375.";
RL   DNA Seq. 7:301-306(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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         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; Z80110; CAB02200.1; -; Genomic_DNA.
DR   EMBL; AE017126; AAP99297.1; -; Genomic_DNA.
DR   RefSeq; NP_874645.1; NC_005042.1.
DR   RefSeq; WP_011124406.1; NC_005042.1.
DR   AlphaFoldDB; P72208; -.
DR   SMR; P72208; -.
DR   STRING; 167539.Pro_0251; -.
DR   EnsemblBacteria; AAP99297; AAP99297; Pro_0251.
DR   GeneID; 54199610; -.
DR   KEGG; pma:Pro_0251; -.
DR   PATRIC; fig|167539.5.peg.259; -.
DR   eggNOG; COG2988; Bacteria.
DR   HOGENOM; CLU_083292_0_0_3; -.
DR   OMA; THGNEIN; -.
DR   OrthoDB; 632656at2; -.
DR   Proteomes; UP000001420; 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..307
FT                   /note="Probable aspartoacylase"
FT                   /id="PRO_0000216878"
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         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT   CONFLICT        71
FT                   /note="L -> V (in Ref. 1; CAB02200)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230..233
FT                   /note="KDIQ -> GDNP (in Ref. 1; CAB02200)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   307 AA;  34328 MW;  8225DAC233D01C35 CRC64;
     MSGIQVLLVA GTHGNEINAP WLFEQWKQKD SLINTHNINI QTVIGNPVAL EQGKRYVDRD
     LNRSFRKDLL LSSDLNAAEH FRALELVSEY GPNGNNPCQI AIDFHSTTSS MGSSLVVYGR
     RPADLAIVSL IQNHLGLPIY LHEGDNAQSG FLVESWPCGF VVEVGPVPQG LLHFQIINQT
     LLTLDSCLKE ISNVINSKTV YPEQLIVHRH LKNIDFPRDS SGVPSSLVHK DIQGRDWYPI
     KNGHPLFESL SGDLTLLLEG GLEEEFVPVF INEAAYAEKN IAMSLTKKEM WDVQKDWIND
     LSKLLNP