ASPA_NOSS1
ID ASPA_NOSS1 Reviewed; 294 AA.
AC Q8YQC1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=alr3912;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB75611.1; -; Genomic_DNA.
DR PIR; AI2294; AI2294.
DR RefSeq; WP_010998053.1; NZ_RSCN01000043.1.
DR AlphaFoldDB; Q8YQC1; -.
DR SMR; Q8YQC1; -.
DR STRING; 103690.17133046; -.
DR EnsemblBacteria; BAB75611; BAB75611; BAB75611.
DR KEGG; ana:alr3912; -.
DR eggNOG; COG2988; Bacteria.
DR OMA; THGNEIN; -.
DR OrthoDB; 632656at2; -.
DR Proteomes; UP000002483; 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..294
FT /note="Probable aspartoacylase"
FT /id="PRO_0000216877"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 63..64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
SQ SEQUENCE 294 AA; 32846 MW; 58BC4450CED55A66 CRC64;
MNKINRVAIV GGTHGNEFTG AFLVKKFQQF PEVIQKPSFE TLTILGNPKA FEAGKRYIEK
DLNRCFLTES LQNTNLSSYE DIRAKQIAGV LGAENKPNVD VVIDLHSTTA NMGLSIILGN
QDPFLLKLCA YLSDINPLVK VCYTIPEKGS NFLRSLNKLG FVIEVGAVAQ GVLNAELFQK
TEQLIYTILD YLEQYNRGNI PKINNLLALY KFTGTVDYPR NENGDIQGMI HPDIQFRDYE
PLNPGDPLFL TLDGKAIAYE GTSTVYPIFI NEAAYYEKGI AMLFTEKQLI NPSS