ASPA_PROM9
ID ASPA_PROM9 Reviewed; 301 AA.
AC Q31CV9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-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=PMT9312_0224;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
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., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
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; CP000111; ABB49286.1; -; Genomic_DNA.
DR RefSeq; WP_011375790.1; NC_007577.1.
DR AlphaFoldDB; Q31CV9; -.
DR SMR; Q31CV9; -.
DR STRING; 74546.PMT9312_0224; -.
DR EnsemblBacteria; ABB49286; ABB49286; PMT9312_0224.
DR KEGG; pmi:PMT9312_0224; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_083292_0_0_3; -.
DR OMA; THGNEIN; -.
DR OrthoDB; 632656at2; -.
DR Proteomes; UP000002715; 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; Zinc.
FT CHAIN 1..301
FT /note="Probable aspartoacylase"
FT /id="PRO_1000147940"
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 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00704"
FT BINDING 61..62
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 301 AA; 34801 MW; 0F6ABA26B70C14F7 CRC64;
MTVQRILIVA GTHGNEINPI WAVKQFNRNE NSLKHGIEYE YIIGNPIAYE KGCRYIDADL
NRSFKKSKNY DQNENSFYEI SRANFLVDQF GINGSKPCQI AIDLHTTTAN MGTSIVMYGR
RFKDFCLAAL LQNKFGLPIY LHEKDKSQTG FLVEAWPCGL VIEIGAVAQN FYDPKIINRF
LIIISSLRDE IDKLKKNLIE LPKDLVVHVH QGSVDYPRDE KGDIDGLIHP KRINRDWKMI
KKGDPLFLNS QGIIYKYDGD QFIWPVFIGE VAYKEKQIAM SYTNKEVICS KNEWVQEFHR
L
