ASPA_SYNSC
ID ASPA_SYNSC Reviewed; 304 AA.
AC Q3AM91;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Syncc9605_0517;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) 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: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; CP000110; ABB34291.1; -; Genomic_DNA.
DR RefSeq; WP_011363523.1; NC_007516.1.
DR AlphaFoldDB; Q3AM91; -.
DR SMR; Q3AM91; -.
DR STRING; 110662.Syncc9605_0517; -.
DR EnsemblBacteria; ABB34291; ABB34291; Syncc9605_0517.
DR KEGG; syd:Syncc9605_0517; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_083292_0_0_3; -.
DR OMA; THGNEIN; -.
DR OrthoDB; 632656at2; -.
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..304
FT /note="Probable aspartoacylase"
FT /id="PRO_1000147943"
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 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
SQ SEQUENCE 304 AA; 33021 MW; 175DF25C29C40346 CRC64;
MSSCGVLVVA GTHGNEVNAP WLLQQWQANP DLIDAAGLAV QKVIGNPEAL RRRCRYVDRD
LNRCFLPEQL EQGASGLEFQ RAGELLRLHG PSGEQPCAVA IDLHSTTAAM GNSLVVYGRR
PADLALAALV QGALGLPIYL HEADAQQTGF LVESWPCGLV IEVGPVPQGL LNAGVVEQTR
LGLESCLRAL YQVRQELARL PDALVVHRHL GSRDLPKAEN GEPQALVHPE LQGRDWQNIA
STQAMFRAAD GTDRCEAWVG GEIPVFVNEA AYAEKSIAFS LTRREVWPVE PNWLLALKQL
LAAA
